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2rr3
From Proteopedia
(Difference between revisions)
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</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=2rr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rr3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rr3 RCSB], [http://www.ebi.ac.uk/pdbsum/2rr3 PDBsum]</span></td></tr> | </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=2rr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rr3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rr3 RCSB], [http://www.ebi.ac.uk/pdbsum/2rr3 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/VAPA_HUMAN VAPA_HUMAN]] May play a role in vesicle trafficking.<ref>PMID:11511104</ref> <ref>PMID:19289470</ref> [[http://www.uniprot.org/uniprot/OSBP1_HUMAN OSBP1_HUMAN]] Binds cholesterol and a range of oxysterols. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability.<ref>PMID:15746430</ref> <ref>PMID:18450749</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Fukada, H | + | [[Category: Fukada, H]] |
| - | [[Category: Furuita, K | + | [[Category: Furuita, K]] |
| - | [[Category: Jee, J | + | [[Category: Jee, J]] |
| - | [[Category: Kojima, C | + | [[Category: Kojima, C]] |
| - | [[Category: Mishima, M | + | [[Category: Mishima, M]] |
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
[[Category: Lipid binding]] | [[Category: Lipid binding]] | ||
Revision as of 23:54, 24 December 2014
Solution structure of the complex between human VAP-A MSP domain and human OSBP FFAT motif
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