3nhd - Revision history

OCA at 09:46, 22 May 2024

OCA — Wed, 22 May 2024 09:46:43 GMT

←Older revision		Revision as of 09:46, 22 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3nhd]] is a 2 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=3NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3nhd]] is a 2 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=3NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></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]] 1.92Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [https://pdbe.org/3nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [https://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd 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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [https://pdbe.org/3nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [https://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:00, 21 December 2022

OCA — Wed, 21 Dec 2022 10:00:37 GMT

←Older revision		Revision as of 10:00, 21 December 2022
Line 3:		Line 3:
	<StructureSection load='3nhd' size='340' side='right'caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3nhd' size='340' side='right'caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3nhd]] is a 2 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=3NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nhc\|3nhc]]</div></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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [https://pdbe.org/3nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [https://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd 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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [https://pdbe.org/3nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [https://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[https://omim.org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[https://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[https://omim.org/entry/137440 137440]]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:10581485</ref> <ref>PMID:2564168</ref> <ref>PMID:1363810</ref> <ref>PMID:7902972</ref> <ref>PMID:7699395</ref> <ref>PMID:7783876</ref> <ref>PMID:8797472</ref> <ref>PMID:9786248</ref> <ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[https://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[https://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[https://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>	+	[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[https://omim.org/entry/123400 123400]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[https://omim.org/entry/600072 600072]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[https://omim.org/entry/137440 137440]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:10581485</ref> <ref>PMID:2564168</ref> <ref>PMID:1363810</ref> <ref>PMID:7902972</ref> <ref>PMID:7699395</ref> <ref>PMID:7783876</ref> <ref>PMID:8797472</ref> <ref>PMID:9786248</ref> <ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[https://omim.org/entry/603218 603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[https://omim.org/entry/245300 245300]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[https://omim.org/entry/606688 606688]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref> <ref>PMID:19936054</ref> <ref>PMID:20564047</ref>	+	[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref> <ref>PMID:19936054</ref> <ref>PMID:20564047</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Apostol~~, M I~~]]	+	[[Category: Apostol MI]]
-	[[Category: Eisenberg, D]]	+	[[Category: Eisenberg D]]
-	~~[[Category: Amyloid-like protofibril]]~~	+
-	~~[[Category: Protein fibril~~]]	+

OCA at 18:33, 27 July 2022

OCA — Wed, 27 Jul 2022 18:33:11 GMT

OCA at 09:04, 21 October 2020

OCA — Wed, 21 Oct 2020 09:04:06 GMT

←Older revision		Revision as of 09:04, 21 October 2020
Line 1:		Line 1:

	==GYVLGS segment 127-132 from human prion with V129==		==GYVLGS segment 127-132 from human prion with V129==
-	<StructureSection load='3nhd' size='340' side='right' caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>	+	<StructureSection load='3nhd' size='340' side='right'caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3NHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [http://pdbe.org/3nhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [http://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd 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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [http://pdbe.org/3nhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [http://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Prion\|Prion]]	+	*[[Prion 3D structures\|Prion 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Apostol, M I]]		[[Category: Apostol, M I]]
	[[Category: Eisenberg, D]]		[[Category: Eisenberg, D]]
	[[Category: Amyloid-like protofibril]]		[[Category: Amyloid-like protofibril]]
	[[Category: Protein fibril]]		[[Category: Protein fibril]]

OCA at 14:40, 4 August 2016

OCA — Thu, 04 Aug 2016 14:40:13 GMT

←Older revision		Revision as of 14:40, 4 August 2016
Line 1:		Line 1:
		+
	==GYVLGS segment 127-132 from human prion with V129==		==GYVLGS segment 127-132 from human prion with V129==
	<StructureSection load='3nhd' size='340' side='right' caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3nhd' size='340' side='right' caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [http://www.ebi.ac.uk/pdbsum/3nhd 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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [http://pdbe.org/3nhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [http://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 3nhd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 16:41, 18 December 2014

OCA — Thu, 18 Dec 2014 16:41:33 GMT

←Older revision		Revision as of 16:41, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3nhd~~\| ~~PDB~~=3nhd \| ~~SCENE~~= }}	+	==GYVLGS segment 127-132 from human prion with V129==
-	===~~GYVLGS segment 127~~-~~132 from~~ human prion with ~~V129~~===	+	<StructureSection load='3nhd' size='340' side='right' caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20685658}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NHD FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [http://www.ebi.ac.uk/pdbsum/3nhd PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[http://omim.org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[http://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[http://omim.org/entry/137440 137440]]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:10581485</ref> <ref>PMID:2564168</ref> <ref>PMID:1363810</ref> <ref>PMID:7902972</ref> <ref>PMID:7699395</ref> <ref>PMID:7783876</ref> <ref>PMID:8797472</ref> <ref>PMID:9786248</ref> <ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[http://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[http://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[http://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref> <ref>PMID:19936054</ref> <ref>PMID:20564047</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A single nucleotide polymorphism (SNP) in codon 129 of the human prion gene, leading to a change from methionine to valine at residue 129 of prion protein (PrP), has been shown to be a determinant in the susceptibility to prion disease. However, the molecular basis of this effect remains unexplained. In the current study, we determined crystal structures of prion segments having either Met or Val at residue 129. These 6-residue segments of PrP centered on residue 129 are "steric zippers," pairs of interacting beta-sheets. Both structures of these "homozygous steric zippers" reveal direct intermolecular interactions between Met or Val in one sheet and the identical residue in the mating sheet. These two structures, plus a structure-based model of the heterozygous Met-Val steric zipper, suggest an explanation for the previously observed effects of this locus on prion disease susceptibility and progression.

-	~~==Disease==~~	+	Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.,Apostol MI, Sawaya MR, Cascio D, Eisenberg D J Biol Chem. 2010 Sep 24;285(39):29671-5. Epub 2010 Aug 4. PMID:20685658<ref>PMID:20685658</ref>
-	~~[[http://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain~~ of ~~humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or~~ prion ~~diseases, like: Creutzfeldt-Jakob disease~~ (~~CJD~~), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to ~~occur after consumption of~~ prion-infected foodstuffs.<ref>PMID:19936054</ref><ref>PMID:1671440</ref><ref>PMID:1975028</ref><ref>PMID:8461023</ref><ref>PMID:7902693</ref><ref>PMID:7906019</ref><ref>PMID:7913755</ref><ref>PMID:8909447</ref><ref>PMID:9266722</ref><ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease ~~(CJD) [MIM:[http://omim~~.~~org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million)~~, ~~while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH)~~, ~~corneal transplantation~~, ~~electroencephalographic electrode implantation~~, ~~etc~~.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref><ref>PMID:1671440</ref><ref>PMID:1975028</ref><ref>PMID:8461023</ref><ref>PMID:7902693</ref><ref>PMID:7906019</ref><ref>PMID:7913755</ref><ref>PMID:8909447</ref><ref>PMID:9266722</ref><ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[http://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref><ref>PMID:19927125</ref><ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-~~Straussler disease (GSD) [MIM:[http://omim~~.~~org/entry/137440 137440]]~~. ~~GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>~~PMID:19936054</ref><ref>PMID:19927125</ref><ref>PMID:10581485</ref><ref>PMID:2564168</ref><ref>PMID:1363810</ref><ref>PMID:7902972</ref><ref>PMID:7699395</ref><ref>PMID:7783876</ref><ref>PMID:8797472</ref><ref>PMID:9786248</ref><ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[http://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[http://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[http://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:~~19936054~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http://www.uniprot.org/uniprot~~/~~PRIO_HUMAN PRIO_HUMAN]] May play~~ a ~~role in neuronal development and synaptic plasticity~~. ~~May be required for neuronal myelin sheath maintenance~~. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of ~~its heparan sulfate side chains (By similarity)~~.<~~ref~~>~~PMID:12732622~~</~~ref~~>~~<ref>PMID:19936054</ref><ref>PMID:20564047</ref>~~	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA].~~	+

	==See Also==		==See Also==
	*[[Prion\|Prion]]		*[[Prion\|Prion]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020685658</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Apostol, M I.]]	+	</StructureSection>
-	[[Category: Eisenberg, D.]]	+	[[Category: Apostol, M I]]
		+	[[Category: Eisenberg, D]]
	[[Category: Amyloid-like protofibril]]		[[Category: Amyloid-like protofibril]]
	[[Category: Protein fibril]]		[[Category: Protein fibril]]

OCA at 20:36, 24 March 2013

OCA — Sun, 24 Mar 2013 20:36:36 GMT

←Older revision		Revision as of 20:36, 24 March 2013
Line 1:		Line 1:
-	[[Image:3nhd.png\|left\|200px]]
-
	{{STRUCTURE_3nhd\| PDB=3nhd \| SCENE= }}		{{STRUCTURE_3nhd\| PDB=3nhd \| SCENE= }}
-
	===GYVLGS segment 127-132 from human prion with V129===		===GYVLGS segment 127-132 from human prion with V129===
		+	{{ABSTRACT_PUBMED_20685658}}

-	~~{{ABSTRACT_PUBMED_20685658}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref><ref>PMID:1671440</ref><ref>PMID:1975028</ref><ref>PMID:8461023</ref><ref>PMID:7902693</ref><ref>PMID:7906019</ref><ref>PMID:7913755</ref><ref>PMID:8909447</ref><ref>PMID:9266722</ref><ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[http://omim.org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref><ref>PMID:1671440</ref><ref>PMID:1975028</ref><ref>PMID:8461023</ref><ref>PMID:7902693</ref><ref>PMID:7906019</ref><ref>PMID:7913755</ref><ref>PMID:8909447</ref><ref>PMID:9266722</ref><ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[http://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref><ref>PMID:19927125</ref><ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[http://omim.org/entry/137440 137440]]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref><ref>PMID:19927125</ref><ref>PMID:10581485</ref><ref>PMID:2564168</ref><ref>PMID:1363810</ref><ref>PMID:7902972</ref><ref>PMID:7699395</ref><ref>PMID:7783876</ref><ref>PMID:8797472</ref><ref>PMID:9786248</ref><ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[http://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[http://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[http://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref><ref>PMID:19936054</ref><ref>PMID:20564047</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020685658</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020685658</ref><references group="xtra"/><references/>
	[[Category: Apostol, M I.]]		[[Category: Apostol, M I.]]
	[[Category: Eisenberg, D.]]		[[Category: Eisenberg, D.]]
	[[Category: Amyloid-like protofibril]]		[[Category: Amyloid-like protofibril]]
	[[Category: Protein fibril]]		[[Category: Protein fibril]]

OCA at 15:30, 20 October 2012

OCA — Sat, 20 Oct 2012 15:30:11 GMT

←Older revision		Revision as of 15:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3nhd]] is a 2 chain structure ~~of [[Prion]]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA].	+	[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA].

	==See Also==		==See Also==

OCA at 18:35, 26 July 2012

OCA — Thu, 26 Jul 2012 18:35:09 GMT

←Older revision		Revision as of 18:35, 26 July 2012
Line 1:		Line 1:
	[[Image:3nhd.png\|left\|200px]]		[[Image:3nhd.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3nhd", 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_3nhd\| PDB=3nhd \| SCENE= }}		{{STRUCTURE_3nhd\| PDB=3nhd \| SCENE= }}

	===GYVLGS segment 127-132 from human prion with V129===		===GYVLGS segment 127-132 from human prion with V129===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20685658}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20685658 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20685658}}		{{ABSTRACT_PUBMED_20685658}}

	==About this Structure==		==About this Structure==
-	[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA].	+	[[3nhd]] is a 2 chain structure of [[Prion]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA].
		+
		+	==See Also==
		+	*[[Prion\|Prion]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20685658~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020685658</ref><references group="xtra"/>
	[[Category: Apostol, M I.]]		[[Category: Apostol, M I.]]
	[[Category: Eisenberg, D.]]		[[Category: Eisenberg, D.]]
		+	[[Category: Amyloid-like protofibril]]
		+	[[Category: Protein fibril]]

OCA: Protected "3nhd" [edit=sysop:move=sysop]

OCA — Wed, 05 Jan 2011 15:41:00 GMT

Protected "3nhd" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:41, 5 January 2011

←Older revision		Revision as of 18:33, 27 July 2022
Line 3:		Line 3:
	<StructureSection load='3nhd' size='340' side='right'caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3nhd' size='340' side='right'caption='[[3nhd]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3nhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NHD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3nhc\|3nhc]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nhc\|3nhc]]</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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [~~http~~://pdbe.org/3nhd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd 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=3nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhd OCA], [https://pdbe.org/3nhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nhd RCSB], [https://www.ebi.ac.uk/pdbsum/3nhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[~~http~~://omim.org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[~~http~~://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[~~http~~://omim.org/entry/137440 137440]]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:10581485</ref> <ref>PMID:2564168</ref> <ref>PMID:1363810</ref> <ref>PMID:7902972</ref> <ref>PMID:7699395</ref> <ref>PMID:7783876</ref> <ref>PMID:8797472</ref> <ref>PMID:9786248</ref> <ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[~~http~~://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[~~http~~://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[~~http~~://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>	+	[[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:[https://omim.org/entry/123400 123400]]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.<ref>PMID:19936054</ref> <ref>PMID:1671440</ref> <ref>PMID:1975028</ref> <ref>PMID:8461023</ref> <ref>PMID:7902693</ref> <ref>PMID:7906019</ref> <ref>PMID:7913755</ref> <ref>PMID:8909447</ref> <ref>PMID:9266722</ref> <ref>PMID:10790216</ref> Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:[https://omim.org/entry/600072 600072]]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:1347910</ref> Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:[https://omim.org/entry/137440 137440]]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.<ref>PMID:19936054</ref> <ref>PMID:19927125</ref> <ref>PMID:10581485</ref> <ref>PMID:2564168</ref> <ref>PMID:1363810</ref> <ref>PMID:7902972</ref> <ref>PMID:7699395</ref> <ref>PMID:7783876</ref> <ref>PMID:8797472</ref> <ref>PMID:9786248</ref> <ref>PMID:11709001</ref> Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:[https://omim.org/entry/603218 603218]]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.<ref>PMID:19936054</ref> Defects in PRNP are the cause of kuru (KURU) [MIM:[https://omim.org/entry/245300 245300]]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.<ref>PMID:19936054</ref> Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:[https://omim.org/entry/606688 606688]]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.<ref>PMID:19936054</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref> <ref>PMID:19936054</ref> <ref>PMID:20564047</ref>	+	[[https://www.uniprot.org/uniprot/PRIO_HUMAN PRIO_HUMAN]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:12732622</ref> <ref>PMID:19936054</ref> <ref>PMID:20564047</ref>
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	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==