1nmj - Revision history

OCA at 18:53, 29 November 2023

OCA — Wed, 29 Nov 2023 18:53:35 GMT

←Older revision		Revision as of 18:53, 29 November 2023
Line 1:		Line 1:

	==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==		==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==
-	<StructureSection load='1nmj' size='340' side='right'caption='[[1nmj~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1nmj' size='340' side='right'caption='[[1nmj]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMJ 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;'>[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [https://pdbe.org/1nmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [https://www.ebi.ac.uk/pdbsum/1nmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmj 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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [https://pdbe.org/1nmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [https://www.ebi.ac.uk/pdbsum/1nmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A4_RAT A4_RAT]] 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 (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). 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 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 (By similarity). Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis (By similarity). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).	+	[https://www.uniprot.org/uniprot/A4_RAT A4_RAT] 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 (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). 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 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 (By similarity). Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis (By similarity). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Huang, J~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Tang, W X~~]]	+	[[Category: Huang J]]
-	[[Category: ~~Yao, Y~~]]	+	[[Category: Tang WX]]
-	[[Category: ~~Amyloid]]~~	+	[[Category: Yao Y]]
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 09:52, 12 May 2021

OCA — Wed, 12 May 2021 09:52:24 GMT

←Older revision		Revision as of 09:52, 12 May 2021
Line 3:		Line 3:
	<StructureSection load='1nmj' size='340' side='right'caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1nmj' size='340' side='right'caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</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;'>[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</div></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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [~~http~~://pdbe.org/1nmj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1nmj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmj 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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [https://pdbe.org/1nmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [https://www.ebi.ac.uk/pdbsum/1nmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/A4_RAT A4_RAT]] 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 (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). 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 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 (By similarity). Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis (By similarity). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).	+	[[https://www.uniprot.org/uniprot/A4_RAT A4_RAT]] 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 (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). 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 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 (By similarity). Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis (By similarity). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 06:41, 7 August 2019

OCA — Wed, 07 Aug 2019 06:41:45 GMT

←Older revision		Revision as of 06:41, 7 August 2019
Line 1:		Line 1:

	==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==		==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==
-	<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1nmj' size='340' side='right'caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 1nmj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1nmj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Amyloid precursor protein 3D structures\|Amyloid precursor protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Huang, J]]		[[Category: Huang, J]]
	[[Category: Tang, W X]]		[[Category: Tang, W X]]

OCA at 09:51, 1 November 2017

OCA — Wed, 01 Nov 2017 09:51:49 GMT

←Older revision		Revision as of 09:51, 1 November 2017
Line 1:		Line 1:
		+
	==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==		==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==
	<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://pdbe.org/1nmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj 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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://pdbe.org/1nmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 1nmj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1nmj" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Amyloid precursor protein\|Amyloid precursor protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:24, 10 September 2015

OCA — Thu, 10 Sep 2015 18:24:58 GMT

←Older revision		Revision as of 18:24, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj 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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://pdbe.org/1nmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	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 1nmj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Huang, J]]		[[Category: Huang, J]]
	[[Category: Tang, W X]]		[[Category: Tang, W X]]

OCA at 04:16, 25 December 2014

OCA — Thu, 25 Dec 2014 04:16:55 GMT

←Older revision		Revision as of 04:16, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj 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=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A4_RAT A4_RAT]] 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 (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). 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 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 (By similarity). Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity). Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis (By similarity). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Huang, J.]]	+	[[Category: Huang, J]]
-	[[Category: Tang, W X.]]	+	[[Category: Tang, W X]]
-	[[Category: Yao, Y.]]	+	[[Category: Yao, Y]]
	[[Category: Amyloid]]		[[Category: Amyloid]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]

OCA at 14:52, 28 September 2014

OCA — Sun, 28 Sep 2014 14:52:33 GMT

←Older revision		Revision as of 14:52, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1nmj.~~png~~\|~~left~~\|~~200px~~]]	+	==The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain==
		+	<StructureSection load='1nmj' size='340' side='right' caption='[[1nmj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMJ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amb\|1amb]], [[1amc\|1amc]], [[1bjb\|1bjb]], [[1bjc\|1bjc]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nmj RCSB], [http://www.ebi.ac.uk/pdbsum/1nmj PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The amyloid beta-peptide (Abeta) is a major component of insoluble amyloid deposits in Alzheimer's disease, and the ability of the beta-peptide to exist in different conformations is dependent on residues 1-28 [beta-(1-28)]. However, different from humans, no Abeta amyloid deposition has been found in aged rats' brains. Studying the three-dimensional solution structure of rat Abeta-(1-28) and the binding circumstance of Zn(2+) is beneficial to a clear understanding of the potential role of Zn(2+) in Alzheimer-associated neuropathogenesis and to suggest why there is no amyloid deposition in aged rats' brains. Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the solution structure of rat Abeta-(1-28) and the binding constant of Zn(2+) to rat Abeta-(1-28). Our results suggest that (1) the three-dimensional solution structure of rat Abeta-(1-28) is more stable than that of human Abeta-(1-28) in DMSO- d(6) and that a helical region from Glu16 to Val24 exists in the rat Abeta-(1-28); (2) the affinity of Zn(2+) for rat Abeta-(1-28) is lower than that for human Abeta-(1-28) and the NMR data suggest that Arg13, His6, and His14 residues provide the primary binding sites for Zn(2+); and (3) the proper binding of Zn(2+) to rat Abeta-(1-28) can induce the peptide to change to a more stable conformation.

-	~~{{STRUCTURE_1nmj\| PDB=1nmj \| SCENE= }}~~	+	The solution structure of rat Abeta-(1-28) and its interaction with zinc ion: insights into the scarcity of amyloid deposition in aged rat brain.,Huang J, Yao Y, Lin J, Ye YH, Sun WY, Tang Dagger WX J Biol Inorg Chem. 2004 Jul;9(5):627-35. Epub 2004 May 25. PMID:15160315<ref>PMID:15160315</ref>

-	~~===The Solution Structure~~ of ~~Rat Ab-(1-28) and its Interaction with Zinc: Insights into~~ the ~~Scarity~~ of ~~Amyloid Deposition in Aged Rat Brain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_15160315}}~~	+	==See Also==
-		+	*[[Amyloid precursor protein\|Amyloid precursor protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1nmj~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Huang, J.]]		[[Category: Huang, J.]]

OCA: Protected "1nmj" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 20:40:13 GMT

Protected "1nmj" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:40, 5 December 2012

OCA at 20:40, 5 December 2012

OCA — Wed, 05 Dec 2012 20:40:09 GMT

←Older revision		Revision as of 20:40, 5 December 2012
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-	{{Seed}}
	[[Image:1nmj.png\|left\|200px]]		[[Image:1nmj.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1nmj", creates the "Structure Box" on the page.
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-	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_1nmj\| PDB=1nmj \| SCENE= }}		{{STRUCTURE_1nmj\| PDB=1nmj \| SCENE= }}

	===The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain===		===The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15160315}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15160315 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15160315}}		{{ABSTRACT_PUBMED_15160315}}

	==About this Structure==		==About this Structure==
-	~~1NMJ is a~~ [[~~Single protein~~]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].	+	[[1nmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].
-		+
-	~~==Reference==~~	+
-	The solution structure of rat Abeta-(1-28) and its interaction with zinc ion: insights into the scarcity of amyloid deposition in aged rat brain., Huang J, Yao Y, Lin J, Ye YH, Sun WY, Tang Dagger WX, J Biol Inorg Chem. 2004 Jul;9(5):627-35. Epub 2004 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15160315 15160315]	+
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Single protein]]
	[[Category: Huang, J.]]		[[Category: Huang, J.]]
	[[Category: Tang, W X.]]		[[Category: Tang, W X.]]
Line 31:		Line 15:
	[[Category: Amyloid]]		[[Category: Amyloid]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
-		+	[[Category: Membrane protein]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Jul 28 09:49:49 2008''~~	+

OCA at 06:49, 28 July 2008

OCA — Mon, 28 Jul 2008 06:49:52 GMT

←Older revision		Revision as of 06:49, 28 July 2008
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-	[[Image:1nmj.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1nmj.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1nmj\| PDB=1nmj \| SCENE= }}		{{STRUCTURE_1nmj\| PDB=1nmj \| SCENE= }}

-	~~'''~~The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain~~'''~~	+	===The Solution Structure of Rat Ab-(1-28) and its Interaction with Zinc: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain===


-	~~==Overview==~~	+	<!--
-	The ~~amyloid beta-peptide (Abeta) is a major component of insoluble amyloid deposits in Alzheimer's disease~~, ~~and the ability of the beta-peptide to exist in different conformations is dependent on residues 1-28 [beta-(1-28)]. However~~, ~~different from humans, no Abeta amyloid deposition has been found in aged rats' brains. Studying~~ the ~~three-dimensional solution structure of rat Abeta-(1-28) and the binding circumstance of Zn(2+) is beneficial~~ to ~~a clear understanding of~~ the ~~potential role of Zn~~(~~2+) in Alzheimer-associated neuropathogenesis and to suggest why there is no amyloid deposition in aged rats' brains~~. ~~Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the solution structure of rat Abeta-(1-28) and the binding constant of Zn(2+) to rat Abeta-(1-28)~~. ~~Our results suggest that (1) the three-dimensional solution structure of rat Abeta-(1-28~~) is ~~more stable than that of human Abeta-(1-28) in DMSO- d(6) and that a helical region from Glu16 to Val24 exists in~~ the ~~rat Abeta~~-(1-28); (2) the affinity of Zn(2+) for rat Abeta-(1-28) is lower than that for human Abeta-(1-28) and the NMR data suggest that Arg13, His6, and His14 residues provide the primary binding sites for Zn(2+); and (3) the proper binding of Zn(2+) to rat Abeta-(1-28) can induce the peptide to change to a more stable conformation.	+	The line below this paragraph, {{ABSTRACT_PUBMED_15160315}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 15160315 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_15160315}}

	==About this Structure==		==About this Structure==
-	1NMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].	+	1NMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMJ OCA].

	==Reference==		==Reference==
Line 27:		Line 31:
	[[Category: Amyloid]]		[[Category: Amyloid]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:42:42 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:49:49 2008''