3hjx - Revision history

OCA at 12:00, 13 October 2021

OCA — Wed, 13 Oct 2021 12:00:32 GMT

←Older revision		Revision as of 12:00, 13 October 2021
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	==Human prion protein variant D178N with V129==		==Human prion protein variant D178N with V129==
-	<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3hjx' size='340' side='right'caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hjx]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HJX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [~~http~~://pdbe.org/3hjx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hjx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hjx 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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [https://pdbe.org/3hjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [https://www.ebi.ac.uk/pdbsum/3hjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hjx 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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/3hjx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/3hjx_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3hjx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3hjx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Prion 3D structures\|Prion 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Antony, L]]		[[Category: Antony, L]]
	[[Category: Hartmann, R]]		[[Category: Hartmann, R]]

OCA at 07:39, 1 November 2017

OCA — Wed, 01 Nov 2017 07:39:35 GMT

←Older revision		Revision as of 07:39, 1 November 2017
Line 1:		Line 1:
		+
	==Human prion protein variant D178N with V129==		==Human prion protein variant D178N with V129==
	<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [http://pdbe.org/3hjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [http://www.ebi.ac.uk/pdbsum/3hjx 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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [http://pdbe.org/3hjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [http://www.ebi.ac.uk/pdbsum/3hjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hjx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3hjx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3hjx" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Prion\|Prion]]
	== References ==		== References ==
	<references/>		<references/>
Line 55:		Line 53:
	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
		+	[[Category: Polymorphism]]
	[[Category: Prion]]		[[Category: Prion]]
	[[Category: Prion protein]]		[[Category: Prion protein]]

OCA at 15:41, 8 February 2016

OCA — Mon, 08 Feb 2016 15:41:23 GMT

←Older revision		Revision as of 15:41, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HJX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [http://www.ebi.ac.uk/pdbsum/3hjx 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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [http://pdbe.org/3hjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [http://www.ebi.ac.uk/pdbsum/3hjx PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hjx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 30:
	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 3hjx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Antony, L]]		[[Category: Antony, L]]
	[[Category: Hartmann, R]]		[[Category: Hartmann, R]]

OCA at 17:58, 18 December 2014

OCA — Thu, 18 Dec 2014 17:58:24 GMT

←Older revision		Revision as of 17:58, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3hjx~~\| ~~PDB~~=3hjx \| ~~SCENE~~= }}	+	==Human prion protein variant D178N with V129==
-	===~~Human prion~~ protein ~~variant D178N with V129~~===	+	<StructureSection load='3hjx' size='340' side='right' caption='[[3hjx]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19927125}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3hjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HJX FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3haf\|3haf]], [[3hak\|3hak]], [[3heq\|3heq]], [[3her\|3her]], [[3hes\|3hes]], [[3hj5\|3hj5]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRNP, PRIP, PRP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hjx RCSB], [http://www.ebi.ac.uk/pdbsum/3hjx 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>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/3hjx_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants: three of wild-type (WT) PrP containing V129, and four of the familial variants D178N and F198S, containing either M129 or V129. Comparison of these structures with each other and with previously published WT PrP structures containing M129 revealed that only WT PrPs were found to crystallize as domain-swapped dimers or closed monomers; the four mutant PrPs crystallized as non-swapped dimers. Three of the four mutant PrPs aligned to form intermolecular beta-sheets. Several regions of structural variability were identified, and analysis of their conformations provides an explanation for the structural features, which can influence the formation and conformation of intermolecular beta-sheets involving the M/V129 polymorphic residue.

-	~~==Disease==~~	+	Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.,Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC EMBO J. 2010 Jan 6;29(1):251-62. Epub 2009 Nov 19. PMID:19927125<ref>PMID:19927125</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==~~	+
-	[[3hjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].	+

	==See Also==		==See Also==
	*[[Prion\|Prion]]		*[[Prion\|Prion]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019927125</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Antony, L.]]	+	[[Category: Antony, L]]
-	[[Category: Hartmann, R.]]	+	[[Category: Hartmann, R]]
-	[[Category: Knaus, K J.]]	+	[[Category: Knaus, K J]]
-	[[Category: Lee, S.]]	+	[[Category: Lee, S]]
-	[[Category: Surewicz, K.]]	+	[[Category: Surewicz, K]]
-	[[Category: Surewicz, W K.]]	+	[[Category: Surewicz, W K]]
-	[[Category: Yee, V C.]]	+	[[Category: Yee, V C]]
	[[Category: Cell membrane]]		[[Category: Cell membrane]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]

OCA at 17:57, 24 March 2013

OCA — Sun, 24 Mar 2013 17:57:13 GMT

←Older revision		Revision as of 17:57, 24 March 2013
Line 1:		Line 1:
-	[[Image:3hjx.png\|left\|200px]]
-
	{{STRUCTURE_3hjx\| PDB=3hjx \| SCENE= }}		{{STRUCTURE_3hjx\| PDB=3hjx \| SCENE= }}
-
	===Human prion protein variant D178N with V129===		===Human prion protein variant D178N with V129===
		+	{{ABSTRACT_PUBMED_19927125}}

-	~~{{ABSTRACT_PUBMED_19927125}}~~	+	==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:019927125</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019927125</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Antony, L.]]		[[Category: Antony, L.]]

OCA at 10:38, 20 October 2012

OCA — Sat, 20 Oct 2012 10:38:26 GMT

←Older revision		Revision as of 10:38, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3hjx]] is a 1 chain structure ~~of [[Prion]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].	+	[[3hjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].

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

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

OCA — Thu, 26 Jul 2012 02:47:52 GMT

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

←Older revision

Revision as of 02:47, 26 July 2012

OCA at 02:47, 26 July 2012

OCA — Thu, 26 Jul 2012 02:47:46 GMT

←Older revision		Revision as of 02:47, 26 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3hjx.png\|left\|200px]]
-	[[Image:3hjx.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3hjx", 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_3hjx\| PDB=3hjx \| SCENE= }}		{{STRUCTURE_3hjx\| PDB=3hjx \| SCENE= }}

	===Human prion protein variant D178N with V129===		===Human prion protein variant D178N with V129===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19927125}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19927125 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19927125}}		{{ABSTRACT_PUBMED_19927125}}

	==About this Structure==		==About this Structure==
-	~~3HJX~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].	+	[[3hjx]] is a 1 chain structure of [[Prion]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].
		+
		+	==See Also==
		+	*[[Prion\|Prion]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19927125~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019927125</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Antony, L.]]		[[Category: Antony, L.]]
Line 41:		Line 32:
	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
-	[[Category: Polymorphism]]
	[[Category: Prion]]		[[Category: Prion]]
	[[Category: Prion protein]]		[[Category: Prion protein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 14:00:53 2010''

OCA at 12:00, 13 January 2010

OCA — Wed, 13 Jan 2010 12:00:54 GMT

←Older revision		Revision as of 12:00, 13 January 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3hjx.jpg\|left\|200px]]

-	The ~~entry 3hjx~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3hjx", 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_3hjx\| PDB=3hjx \| SCENE= }}

-	~~Authors: Yee, V.C., Lee, S.~~	+	===Human prion protein variant D178N with V129===

-	Description: Prion protein variant

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jul 8 09:~~14:~~42 2009~~''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19927125}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19927125 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19927125}}
		+
		+	==About this Structure==
		+	3HJX is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJX OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19927125</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Antony, L.]]
		+	[[Category: Hartmann, R.]]
		+	[[Category: Knaus, K J.]]
		+	[[Category: Lee, S.]]
		+	[[Category: Surewicz, K.]]
		+	[[Category: Surewicz, W K.]]
		+	[[Category: Yee, V C.]]
		+	[[Category: Cell membrane]]
		+	[[Category: Disease mutation]]
		+	[[Category: Disulfide bond]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Golgi apparatus]]
		+	[[Category: Gpi-anchor]]
		+	[[Category: Lipoprotein]]
		+	[[Category: Membrane]]
		+	[[Category: Membrane protein]]
		+	[[Category: Polymorphism]]
		+	[[Category: Prion]]
		+	[[Category: Prion protein]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 14:00:53 2010''

OCA at 06:14, 8 July 2009

OCA — Wed, 08 Jul 2009 06:14:42 GMT

←Older revision		Revision as of 06:14, 8 July 2009
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3hjx is ON HOLD	+	The entry 3hjx is ON HOLD until Paper Publication

	Authors: Yee, V.C., Lee, S.		Authors: Yee, V.C., Lee, S.
Line 7:		Line 7:
	Description: Prion protein variant		Description: Prion protein variant

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jun~~ ~~4 07~~:18:37 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 8 09:14:42 2009''