View source for 4bvm


==The peripheral membrane protein P2 from human myelin at atomic resolution==
<StructureSection load='4bvm' size='340' side='right'caption='[[4bvm]], [[Resolution|resolution]] 0.93&Aring;' scene=''>
== 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://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>
== 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 ==
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bvm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Kursula, P]]
[[Category: Ruskamo, S]]
[[Category: Yadav, R P]]
[[Category: Fabp]]
[[Category: Membrane protein]]
[[Category: Ultrahigh resolution]]