4bvm - Revision history

OCA at 11:58, 20 December 2023

2023-12-20T11:58:56Z

← Older revision		Revision as of 11:58, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 0.93Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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'>[https://proteopedia.org/fgij/fg.htm?mol=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [https://pdbe.org/4bvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [https://www.ebi.ac.uk/pdbsum/4bvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvm 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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [https://pdbe.org/4bvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [https://www.ebi.ac.uk/pdbsum/4bvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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>		[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;">
			== Publication Abstract from PubMed ==
			P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 A allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.

			Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.,Ruskamo S, Yadav RP, Sharma S, Lehtimaki M, Laulumaa S, Aggarwal S, Simons M, Burck J, Ulrich AS, Juffer AH, Kursula I, Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):165-76. doi:, 10.1107/S1399004713027910. Epub 2013 Dec 31. PMID:24419389<ref>PMID:24419389</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4bvm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:11, 7 September 2022

2022-09-07T17:11:16Z

← Older revision		Revision as of 17:11, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4bvm' size='340' side='right'caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>		<StructureSection load='4bvm' size='340' side='right'caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [~~http~~://pdbe.org/4bvm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bvm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvm 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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [https://pdbe.org/4bvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [https://www.ebi.ac.uk/pdbsum/4bvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvm 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;">~~
	~~== Publication Abstract from PubMed ==~~
	P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 A allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.

	Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.,Ruskamo S, Yadav RP, Sharma S, Lehtimaki M, Laulumaa S, Aggarwal S, Simons M, Burck J, Ulrich AS, Juffer AH, Kursula I, Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):165-76. doi:, 10.1107/S1399004713027910. Epub 2013 Dec 31. PMID:24419389<ref>PMID:24419389</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4bvm" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>
	__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: Yadav~~, R P]]~~		[[Category: Yadav RP]]
	~~[[Category: Fabp]]~~
	~~[[Category: Membrane protein]]~~
	~~[[Category: Ultrahigh resolution~~]]

OCA at 17:03, 29 January 2020

2020-01-29T17:03:43Z

← Older revision		Revision as of 17:03, 29 January 2020
Line 1:		Line 1:

	==The peripheral membrane protein P2 from human myelin at atomic resolution==		==The peripheral membrane protein P2 from human myelin at atomic resolution==
	<StructureSection load='4bvm' size='340' side='right' caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>		<StructureSection load='4bvm' size='340' side='right'caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BVM FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Kursula, P]]		[[Category: Kursula, P]]
	[[Category: Ruskamo, S]]		[[Category: Ruskamo, S]]

OCA at 14:55, 5 August 2016

2016-08-05T14:55:24Z

← Older revision		Revision as of 14:55, 5 August 2016
Line 1:		Line 1:

	==The peripheral membrane protein P2 from human myelin at atomic resolution==		==The peripheral membrane protein P2 from human myelin at atomic resolution==
	<StructureSection load='4bvm' size='340' side='right' caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>		<StructureSection load='4bvm' size='340' side='right' caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=CIT:CITRIC+ACID'>CIT</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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [http://www.ebi.ac.uk/pdbsum/4bvm 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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [http://pdbe.org/4bvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [http://www.ebi.ac.uk/pdbsum/4bvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4bvm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:26, 25 December 2014

2014-12-25T03:26:22Z

← Older revision		Revision as of 03:26, 25 December 2014
Line 6:		Line 6:
	<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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [http://www.ebi.ac.uk/pdbsum/4bvm 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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [http://www.ebi.ac.uk/pdbsum/4bvm PDBsum]</span></td></tr>
	</table>		</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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:23, 21 December 2014

2014-12-21T18:23:35Z

← Older revision		Revision as of 18:23, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4bvm\| PDB=4bvm \| SCENE= }}~~		==The peripheral membrane protein P2 from human myelin at atomic resolution==
	===The peripheral membrane protein P2 from human myelin at atomic resolution===		<StructureSection load='4bvm' size='340' side='right' caption='[[4bvm]], [[Resolution\|resolution]] 0.93Å' scene=''>
	~~{{ABSTRACT_PUBMED_24419389}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4bvm]] 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=4BVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BVM FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=4bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bvm RCSB], [http://www.ebi.ac.uk/pdbsum/4bvm PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 A allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.

	~~==Function==~~		Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.,Ruskamo S, Yadav RP, Sharma S, Lehtimaki M, Laulumaa S, Aggarwal S, Simons M, Burck J, Ulrich AS, Juffer AH, Kursula I, Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):165-76. doi:, 10.1107/S1399004713027910. Epub 2013 Dec 31. PMID:24419389<ref>PMID:24419389</ref>
	~~[[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>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4bvm]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4BVM OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:024419389</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
	[[Category: Kursula, P.]]		</StructureSection>
	[[Category: Ruskamo, S.]]		[[Category: Human]]
	[[Category: Yadav, R P.]]		[[Category: Kursula, P]]
			[[Category: Ruskamo, S]]
			[[Category: Yadav, R P]]
	[[Category: Fabp]]		[[Category: Fabp]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
	[[Category: Ultrahigh resolution]]		[[Category: Ultrahigh resolution]]

OCA at 05:41, 22 January 2014

2014-01-22T05:41:43Z

← Older revision		Revision as of 05:41, 22 January 2014
Line 1:		Line 1:
	{{STRUCTURE_4bvm\| PDB=4bvm \| SCENE= }}		{{STRUCTURE_4bvm\| PDB=4bvm \| SCENE= }}
	===The peripheral membrane protein P2 from human myelin at atomic resolution===		===The peripheral membrane protein P2 from human myelin at atomic resolution===
			{{ABSTRACT_PUBMED_24419389}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
	<references group="xtra"/><references/>		<ref group="xtra">PMID:024419389</ref><references group="xtra"/><references/>
	[[Category: Kursula, P.]]		[[Category: Kursula, P.]]
	[[Category: Ruskamo, S.]]		[[Category: Ruskamo, S.]]

OCA at 08:21, 15 January 2014

2014-01-15T08:21:06Z

← Older revision		Revision as of 08:21, 15 January 2014
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		{{STRUCTURE_4bvm\| PDB=4bvm \| SCENE= }}
			===The peripheral membrane protein P2 from human myelin at atomic resolution===

	~~The entry 4bvm is ON HOLD~~ ~~until Paper Publication~~		==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>

	~~Authors~~: ~~Ruskamo, S~~.~~, Yadav, R~~.P.~~, Kursula, P~~.		==About this Structure==
			[[4bvm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BVM OCA].

	~~Description~~: ~~The peripheral membrane~~ protein ~~P2 from human myelin at atomic~~ resolution		==Reference==
			<references group="xtra"/><references/>
			[[Category: Kursula, P.]]
			[[Category: Ruskamo, S.]]
			[[Category: Yadav, R P.]]
			[[Category: Fabp]]
			[[Category: Membrane protein]]
			[[Category: Ultrahigh resolution]]

OCA at 08:43, 8 January 2014

2014-01-08T08:43:39Z

← Older revision		Revision as of 08:43, 8 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4bvm is ON HOLD		The entry 4bvm is ON HOLD until Paper Publication

	Authors: Ruskamo, S., Yadav, R.P., Kursula, P.		Authors: Ruskamo, S., Yadav, R.P., Kursula, P.

	Description: The peripheral membrane protein P2 from human myelin at atomic resolution		Description: The peripheral membrane protein P2 from human myelin at atomic resolution

OCA: Protected "4bvm" [edit=sysop:move=sysop]

2013-07-03T12:54:04Z

Protected "4bvm" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:54, 3 July 2013
(No difference)