2y3j - Revision history

OCA at 14:02, 1 February 2024

OCA — Thu, 01 Feb 2024 14:02:08 GMT

←Older revision		Revision as of 14:02, 1 February 2024
Line 3:		Line 3:
	<StructureSection load='2y3j' size='340' side='right'caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2y3j' size='340' side='right'caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1uoa\|1uoa]]~~, [[~~1taw~~\|~~1taw~~]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</div></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.99Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [https://pdbe.org/2y3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [https://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [https://pdbe.org/2y3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [https://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>	+	[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>	+	[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Colletier~~, J P~~]]	+	[[Category: Colletier JP]]
-	[[Category: Eisenberg, D]]	+	[[Category: Eisenberg D]]
-	[[Category: Laganowsky, A]]	+	[[Category: Laganowsky A]]
-	[[Category: Sawaya~~, M R]]~~	+	[[Category: Sawaya MR]]
-	~~[[Category: Alzheimer disease]]~~	+
-	~~[[Category: Protein fibril~~]]	+

OCA at 12:22, 27 April 2022

OCA — Wed, 27 Apr 2022 12:22:28 GMT

←Older revision		Revision as of 12:22, 27 April 2022
Line 3:		Line 3:
	<StructureSection load='2y3j' size='340' side='right'caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2y3j' size='340' side='right'caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [~~http~~://pdbe.org/2y3j PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [https://pdbe.org/2y3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [https://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[~~http~~://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[~~http~~://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>	+	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>	+	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:33, 22 July 2020

OCA — Wed, 22 Jul 2020 12:33:09 GMT

←Older revision		Revision as of 12:33, 22 July 2020
Line 1:		Line 1:

	==Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35)==		==Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35)==
-	<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>	+	<StructureSection load='2y3j' size='340' side='right'caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [http://pdbe.org/2y3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [http://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [http://pdbe.org/2y3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [http://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Colletier, J P]]		[[Category: Colletier, J P]]
	[[Category: Eisenberg, D]]		[[Category: Eisenberg, D]]

OCA at 09:20, 10 October 2018

OCA — Wed, 10 Oct 2018 09:20:32 GMT

←Older revision		Revision as of 09:20, 10 October 2018
Line 1:		Line 1:

-	==~~STRUCTURE OF SEGMENT~~ AIIGLM ~~FROM THE AMYLOID~~-~~BETA PEPTIDE~~ (AB, ~~RESIDUES~~ 30-35)==	+	==Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35)==
	<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 15:01, 5 August 2016

OCA — Fri, 05 Aug 2016 15:01:02 GMT

←Older revision		Revision as of 15:01, 5 August 2016
Line 1:		Line 1:
		+
	==STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)==		==STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)==
	<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>		<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [http://www.ebi.ac.uk/pdbsum/2y3j PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [http://pdbe.org/2y3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [http://www.ebi.ac.uk/pdbsum/2y3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3j ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2y3j" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:57, 18 December 2014

OCA — Thu, 18 Dec 2014 13:57:27 GMT

←Older revision		Revision as of 13:57, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2y3j\| PDB=2y3j \| SCENE= }}~~	+	==STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)==
-	===STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)===	+	<StructureSection load='2y3j' size='340' side='right' caption='[[2y3j]], [[Resolution\|resolution]] 1.99Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21949245}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3J FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uoa\|1uoa]], [[1taw\|1taw]], [[1qcm\|1qcm]], [[1tkn\|1tkn]], [[1ba6\|1ba6]], [[1qyt\|1qyt]], [[1bjb\|1bjb]], [[2y3l\|2y3l]], [[2y2a\|2y2a]], [[2y3k\|2y3k]], [[1ca0\|1ca0]], [[1brc\|1brc]], [[1uo8\|1uo8]], [[1ba4\|1ba4]], [[2wk3\|2wk3]], [[1aap\|1aap]], [[1qwp\|1qwp]], [[1x11\|1x11]], [[1ze9\|1ze9]], [[1qxc\|1qxc]], [[1iyt\|1iyt]], [[1ze7\|1ze7]], [[2beg\|2beg]], [[1uoi\|1uoi]], [[1amb\|1amb]], [[1rw6\|1rw6]], [[1uo7\|1uo7]], [[1owt\|1owt]], [[1aml\|1aml]], [[1amc\|1amc]], [[1zjd\|1zjd]], [[2bp4\|2bp4]], [[2bom\|2bom]], [[1bjc\|1bjc]], [[1mwp\|1mwp]], [[2y29\|2y29]], [[1hz3\|1hz3]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3j RCSB], [http://www.ebi.ac.uk/pdbsum/2y3j PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[http://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[http://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Amyloid-beta (Abeta) aggregates are the main constituent of senile plaques, the histological hallmark of Alzheimer's disease. Abeta molecules form beta-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of Abeta has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. To elucidate Abeta polymorphism in atomic detail, we determined eight new microcrystal structures of fiber-forming segments of Abeta. These structures, all of short, self-complementing pairs of beta-sheets termed steric zippers, reveal a variety of modes of self-association of Abeta. Combining these atomic structures with previous NMR studies allows us to propose several fiber models, offering molecular models for some of the repertoire of polydisperse structures accessible to Abeta. These structures and molecular models contribute fundamental information for understanding Abeta polymorphic nature and pathogenesis.

-	~~==Disease==~~	+	Molecular basis for amyloid-{beta} polymorphism.,Colletier JP, Laganowsky A, Landau M, Zhao M, Soriaga AB, Goldschmidt L, Flot D, Cascio D, Sawaya MR, Eisenberg D Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):16938-43. Epub 2011 Sep 23. PMID:21949245<ref>PMID:21949245</ref>
-	~~[[http://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[http://omim.org/entry/104300 104300]]. AD1 is a familial early~~-~~onset form of Alzheimer disease~~. ~~It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia~~, ~~loss of cognitive abilities~~, ~~and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles~~, ~~extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s)~~, derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref><ref>PMID:15201367</ref><ref>PMID:1671712</ref><ref>PMID:1908231</ref><ref>PMID:1678058</ref><ref>PMID:1944558</ref><ref>PMID:1925564</ref><ref>PMID:1415269</ref><ref>PMID:1303239</ref><ref>PMID:1302033</ref><ref>PMID:1303275</ref><ref>PMID:8267572</ref><ref>PMID:8290042</ref><ref>PMID:8577393</ref><ref>PMID:9328472</ref><ref>PMID:9754958</ref><ref>PMID:10097173</ref><ref>PMID:10631141</ref><ref>PMID:10665499</ref><ref>PMID:10867787</ref><ref>PMID:11063718</ref><ref>PMID:11311152</ref><ref>PMID:11528419</ref><ref>PMID:12034808</ref><ref>PMID:15365148</ref><ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[http://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, ~~recurrent strokes~~, ~~cerebral ischemia~~, ~~cerebral infarction~~, ~~and progressive mental deterioration~~. ~~Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque~~-~~like structures~~. ~~They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease~~. ~~Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>~~PMID:~~10821838</ref><ref>PMID:2111584</ref><ref>PMID:11409420</ref><ref>PMID:12654973</ref>~~<ref>PMID:~~16178030~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth~~, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the ~~extracellular matrix such as heparin and collagen I and IV~~. ~~The splice isoforms that contain the BPTI domain possess protease inhibitor activity~~. ~~Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization~~ of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<~~ref~~>~~PMID:9168929~~</~~ref~~><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	~~[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA].~~	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+	[[Category: Colletier, J P]]
-	~~<ref group="xtra">PMID:021949245</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	[[Category: Eisenberg, D]]
-	[[Category: Colletier, J P.]]	+	[[Category: Laganowsky, A]]
-	[[Category: Eisenberg, D.]]	+	[[Category: Sawaya, M R]]
-	[[Category: Laganowsky, A.]]	+
-	[[Category: Sawaya, M R.]]	+
	[[Category: Alzheimer disease]]		[[Category: Alzheimer disease]]
	[[Category: Protein fibril]]		[[Category: Protein fibril]]

OCA at 00:26, 25 March 2013

OCA — Mon, 25 Mar 2013 00:26:33 GMT

←Older revision		Revision as of 00:26, 25 March 2013
Line 1:		Line 1:
-	[[Image:2y3j.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_2y3j", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2y3j\| PDB=2y3j \| SCENE= }}		{{STRUCTURE_2y3j\| PDB=2y3j \| SCENE= }}
-
	===STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)===		===STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)===
		+	{{ABSTRACT_PUBMED_21949245}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[http://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref><ref>PMID:15201367</ref><ref>PMID:1671712</ref><ref>PMID:1908231</ref><ref>PMID:1678058</ref><ref>PMID:1944558</ref><ref>PMID:1925564</ref><ref>PMID:1415269</ref><ref>PMID:1303239</ref><ref>PMID:1302033</ref><ref>PMID:1303275</ref><ref>PMID:8267572</ref><ref>PMID:8290042</ref><ref>PMID:8577393</ref><ref>PMID:9328472</ref><ref>PMID:9754958</ref><ref>PMID:10097173</ref><ref>PMID:10631141</ref><ref>PMID:10665499</ref><ref>PMID:10867787</ref><ref>PMID:11063718</ref><ref>PMID:11311152</ref><ref>PMID:11528419</ref><ref>PMID:12034808</ref><ref>PMID:15365148</ref><ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[http://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref><ref>PMID:2111584</ref><ref>PMID:11409420</ref><ref>PMID:12654973</ref><ref>PMID:16178030</ref>

-	<!--	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21949245}}~~, ~~adds~~ the ~~Publication Abstract~~ to the ~~page~~	+	[[http://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref><ref>PMID:11544248</ref><ref>PMID:11943163</ref><ref>PMID:19225519</ref><ref>PMID:19901339</ref>
-	(as ~~it appears~~ on ~~PubMed at http~~://~~www~~.~~pubmed~~.~~gov~~), ~~where 21949245~~ is the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_21949245}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021949245</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021949245</ref><references group="xtra"/><references/>
	[[Category: Colletier, J P.]]		[[Category: Colletier, J P.]]
	[[Category: Eisenberg, D.]]		[[Category: Eisenberg, D.]]

OCA at 08:20, 2 November 2011

OCA — Wed, 02 Nov 2011 08:20:38 GMT

←Older revision		Revision as of 08:20, 2 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:2y3j.jpg\|left\|200px]]

-	The ~~entry 2y3j~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2y3j", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_2y3j\| PDB=2y3j \| SCENE= }}

-	~~Authors: Colletier~~, ~~J.P., Laganowsky, A., Sawaya, M.R., Eisenberg, D.~~	+	===STRUCTURE OF SEGMENT AIIGLM FROM THE AMYLOID-BETA PEPTIDE (AB, RESIDUES 30-35)===

-	~~Description~~: Structure ~~of segment AIIGLM~~ from ~~the amyloid~~-~~beta peptide (Ab~~, ~~residues 30-35)~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21949245}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21949245 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21949245}}
		+
		+	==About this Structure==
		+	[[2y3j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3J OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021949245</ref><references group="xtra"/>
		+	[[Category: Colletier, J P.]]
		+	[[Category: Eisenberg, D.]]
		+	[[Category: Laganowsky, A.]]
		+	[[Category: Sawaya, M R.]]
		+	[[Category: Alzheimer disease]]
		+	[[Category: Protein fibril]]

OCA: Protected "2y3j" [edit=sysop:move=sysop]

OCA — Wed, 29 Dec 2010 18:06:34 GMT

Protected "2y3j" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:06, 29 December 2010

OCA: New page: '''Unreleased structure''' The entry 2y3j is ON HOLD until Paper Publication Authors: Colletier, J.P., Laganowsky, A., Sawaya, M.R., Eisenberg, D. Description: Structure of segment AII...

OCA — Wed, 29 Dec 2010 18:06:33 GMT

New page: '''Unreleased structure''' The entry 2y3j is ON HOLD until Paper Publication Authors: Colletier, J.P., Laganowsky, A., Sawaya, M.R., Eisenberg, D. Description: Structure of segment AII...

New page

'''Unreleased structure'''

The entry 2y3j is ON HOLD until Paper Publication

Authors: Colletier, J.P., Laganowsky, A., Sawaya, M.R., Eisenberg, D.

Description: Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35)