6i42 - Revision history

OCA at 11:45, 24 January 2024

OCA — Wed, 24 Jan 2024 11:45:55 GMT

←Older revision		Revision as of 11:45, 24 January 2024
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	<StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6i42]] is a 2 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=6I42 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6I42 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6i42]] 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=6I42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I42 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=9606 HUMAN]), SNCA, NACP, PARK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.38Å</td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>~~[~~http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase~~]~~, with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.~~1.~~8 5.2.1.8] </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=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [https://pdbe.org/6i42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [https://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</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=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [~~http~~://pdbe.org/6i42 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN]] Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1. Defects in SNCA are the cause of Parkinson disease type 1 (PARK1) [MIM:[http://omim.org/entry/168601 168601]]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.<ref>PMID:9197268</ref> <ref>PMID:9462735</ref> <ref>PMID:14755719</ref> Defects in SNCA are the cause of Parkinson disease type 4 (PARK4) [MIM:[http://omim.org/entry/605543 605543]]. A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Defects in SNCA are the cause of dementia Lewy body (DLB) [MIM:[http://omim.org/entry/127750 127750]]. A neurodegenerative disorder clinically characterized by mental impairment leading to dementia, parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [[http://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN]] May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.	+	[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 6i42" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6i42" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Alpha-synuclein\|Alpha-synuclein]]
		+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Becker S]]
-	[[Category: Becker, S]]	+	[[Category: Favretto F]]
-	[[Category: Favretto, F]]	+	[[Category: Zweckstetter M]]
-	[[Category: Zweckstetter, M]]	+
-	~~[[Category: Alpha-synuclein]]~~	+
-	~~[[Category: Cyclophilin some]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Peptidyl-prolyl isomerase]]~~	+
-	~~[[Category: Prenac~~]]	+

OCA at 09:28, 1 April 2020

OCA — Wed, 01 Apr 2020 09:28:47 GMT

←Older revision		Revision as of 09:28, 1 April 2020
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	<StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6i42]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I42 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6i42]] is a 2 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=6I42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I42 FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SNCA, NACP, PARK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [http://pdbe.org/6i42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [http://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</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=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [http://pdbe.org/6i42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [http://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 06:17, 19 February 2020

OCA — Wed, 19 Feb 2020 06:17:22 GMT

←Older revision		Revision as of 06:17, 19 February 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6i42 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex==
		+	<StructureSection load='6i42' size='340' side='right'caption='[[6i42]], [[Resolution\|resolution]] 1.38Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6i42]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I42 FirstGlance]. <br>
		+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i42 OCA], [http://pdbe.org/6i42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i42 RCSB], [http://www.ebi.ac.uk/pdbsum/6i42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i42 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN]] Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1. Defects in SNCA are the cause of Parkinson disease type 1 (PARK1) [MIM:[http://omim.org/entry/168601 168601]]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.<ref>PMID:9197268</ref> <ref>PMID:9462735</ref> <ref>PMID:14755719</ref> Defects in SNCA are the cause of Parkinson disease type 4 (PARK4) [MIM:[http://omim.org/entry/605543 605543]]. A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Defects in SNCA are the cause of dementia Lewy body (DLB) [MIM:[http://omim.org/entry/127750 127750]]. A neurodegenerative disorder clinically characterized by mental impairment leading to dementia, parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [[http://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN]] May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peptidylprolyl isomerases (PPIases) catalyze cis/trans isomerization of prolines. The PPIase CypA colocalizes with the Parkinson's disease (PD)-associated protein alpha-synuclein in cells and interacts with alpha-synuclein oligomers. Herein, we describe atomic insights into the molecular details of the alpha-synuclein/CypA interaction. NMR spectroscopy shows that CypA catalyzes isomerization of proline 128 in the C-terminal domain of alpha-synuclein. Strikingly, we reveal a second CypA-binding site formed by the hydrophobic sequence (47) GVVHGVATVA(56) , termed PreNAC. The 1.38 A crystal structure of the CypA/PreNAC complex displays a contact between alanine 53 of alpha-synuclein and glutamine 111 in the catalytic pocket of CypA. Mutation of alanine 53 to glutamate, as found in patients with early-onset PD, weakens the interaction of alpha-synuclein with CypA. Our study provides high-resolution insights into the structure of the PD-associated protein alpha-synuclein in complex with the most abundant cellular cyclophilin.

-	~~Authors~~:	+	The Molecular Basis of the Interaction of Cyclophilin A with alpha-Synuclein.,Favretto F, Baker JD, Strohaker T, Andreas LB, Blair LJ, Becker S, Zweckstetter M Angew Chem Int Ed Engl. 2019 Dec 12. doi: 10.1002/anie.201914878. PMID:31830361<ref>PMID:31830361</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6i42" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Peptidylprolyl isomerase]]
		+	[[Category: Becker, S]]
		+	[[Category: Favretto, F]]
		+	[[Category: Zweckstetter, M]]
		+	[[Category: Alpha-synuclein]]
		+	[[Category: Cyclophilin some]]
		+	[[Category: Isomerase]]
		+	[[Category: Peptidyl-prolyl isomerase]]
		+	[[Category: Prenac]]

OCA at 18:31, 2 December 2018

OCA — Sun, 02 Dec 2018 18:31:41 GMT

←Older revision		Revision as of 18:31, 2 December 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6i42 is ON HOLD	+	The entry 6i42 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6i42" [edit=sysop:move=sysop]

OCA — Wed, 14 Nov 2018 06:23:13 GMT

Protected "6i42" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:23, 14 November 2018

OCA: New page: '''Unreleased structure''' The entry 6i42 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 14 Nov 2018 06:23:11 GMT

New page: '''Unreleased structure''' The entry 6i42 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6i42 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]