5n4p - Revision history

OCA at 18:02, 8 November 2023

2023-11-08T18:02:21Z

←Older revision		Revision as of 18:02, 8 November 2023
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	<StructureSection load='5n4p' size='340' side='right'caption='[[5n4p]], [[Resolution\|resolution]] 1.53Å' scene=''>		<StructureSection load='5n4p' size='340' side='right'caption='[[5n4p]], [[Resolution\|resolution]] 1.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n4p]] 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=5N4P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5N4P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n4p]] is a 1 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=5N4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N4P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</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]] 1.533Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PMP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene></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=5n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4p OCA], [~~http~~://pdbe.org/5n4p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5n4p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5n4p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4p 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=5n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4p OCA], [https://pdbe.org/5n4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n4p RCSB], [https://www.ebi.ac.uk/pdbsum/5n4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MYP2_HUMAN MYP2_HUMAN]] May play a role in lipid transport protein in Schwann cells. May bind cholesterol.<ref>PMID:20421974</ref>	+	[https://www.uniprot.org/uniprot/MYP2_HUMAN MYP2_HUMAN] May play a role in lipid transport protein in Schwann cells. May bind cholesterol.<ref>PMID:20421974</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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kursula, P]]	+	[[Category: Kursula P]]
-	[[Category: Ruskamo, S]]	+	[[Category: Ruskamo S]]
-	~~[[Category: Fatty acid binding protein]]~~	+
-	~~[[Category: Lipid binding protein~~]]	+

OCA at 06:42, 16 October 2019

2019-10-16T06:42:19Z

←Older revision		Revision as of 06:42, 16 October 2019
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	==Human myelin P2, mutant I52T==		==Human myelin P2, mutant I52T==
-	<StructureSection load='5n4p' size='340' side='right' caption='[[5n4p]], [[Resolution\|resolution]] 1.53Å' scene=''>	+	<StructureSection load='5n4p' size='340' side='right'caption='[[5n4p]], [[Resolution\|resolution]] 1.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n4p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n4p]] 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=5N4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PMP2 ([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=5n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4p OCA], [http://pdbe.org/5n4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4p RCSB], [http://www.ebi.ac.uk/pdbsum/5n4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4p 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=5n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4p OCA], [http://pdbe.org/5n4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4p RCSB], [http://www.ebi.ac.uk/pdbsum/5n4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4p ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Kursula, P]]		[[Category: Kursula, P]]
	[[Category: Ruskamo, S]]		[[Category: Ruskamo, S]]
	[[Category: Fatty acid binding protein]]		[[Category: Fatty acid binding protein]]
	[[Category: Lipid binding protein]]		[[Category: Lipid binding protein]]

OCA at 09:10, 9 August 2017

2017-08-09T09:10:40Z

←Older revision		Revision as of 09:10, 9 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5n4p is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Human myelin P2, mutant I52T==
		+	<StructureSection load='5n4p' size='340' side='right' caption='[[5n4p]], [[Resolution\|resolution]] 1.53Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5n4p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4P FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene></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=5n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4p OCA], [http://pdbe.org/5n4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4p RCSB], [http://www.ebi.ac.uk/pdbsum/5n4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4p ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MYP2_HUMAN MYP2_HUMAN]] May play a role in lipid transport protein in Schwann cells. May bind cholesterol.<ref>PMID:20421974</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Charcot-Marie-Tooth (CMT) disease is one of the most common inherited neuropathies. Recently, three CMT1-associated point mutations (I43N, T51P, and I52T) were discovered in the abundant peripheral myelin protein P2. These mutations trigger abnormal myelin structure, leading to reduced nerve conduction velocity, muscle weakness, and distal limb atrophy. P2 is a myelin-specific protein expressed by Schwann cells that binds to fatty acids and membranes, contributing to peripheral myelin lipid homeostasis. We studied the molecular basis of the P2 patient mutations. None of the CMT1-associated mutations alter the overall folding of P2 in the crystal state. P2 disease variants show increased aggregation tendency and remarkably reduced stability, T51P being most severe. In addition, P2 disease mutations affect protein dynamics. Both fatty acid binding by P2 and the kinetics of its membrane interactions are affected by the mutations. Experiments and simulations suggest opening of the beta barrel in T51P, possibly representing a general mechanism in fatty acid-binding proteins. Our findings demonstrate that altered biophysical properties and functional dynamics of P2 may cause myelin defects in CMT1 patients. At the molecular level, a few malformed hydrogen bonds lead to structural instability and misregulation of conformational changes related to ligand exchange and membrane binding.

-	~~Authors: Ruskamo~~, S., ~~Kursula~~, P.	+	Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2.,Ruskamo S, Nieminen T, Kristiansen CK, Vatne GH, Baumann A, Hallin EI, Raasakka A, Joensuu P, Bergmann U, Vattulainen I, Kursula P Sci Rep. 2017 Jul 26;7(1):6510. doi: 10.1038/s41598-017-06781-0. PMID:28747762<ref>PMID:28747762</ref>

-	~~Description: Human myelin P2~~, ~~mutant I52T~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5n4p" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Kursula, P]]		[[Category: Kursula, P]]
	[[Category: Ruskamo, S]]		[[Category: Ruskamo, S]]
		+	[[Category: Fatty acid binding protein]]
		+	[[Category: Lipid binding protein]]

OCA: Protected "5n4p" [edit=sysop:move=sysop]

2017-03-09T12:03:03Z

Protected "5n4p" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:03, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5n4p is ON HOLD until Paper Publication Authors: Ruskamo, S., Kursula, P. Description: Human myelin P2, mutant I52T [[Category: Unreleased Structur...

2017-03-09T12:03:02Z

New page: '''Unreleased structure''' The entry 5n4p is ON HOLD until Paper Publication Authors: Ruskamo, S., Kursula, P. Description: Human myelin P2, mutant I52T [[Category: Unreleased Structur...

New page

'''Unreleased structure'''

The entry 5n4p is ON HOLD until Paper Publication

Authors: Ruskamo, S., Kursula, P.

Description: Human myelin P2, mutant I52T
[[Category: Unreleased Structures]]
[[Category: Kursula, P]]
[[Category: Ruskamo, S]]