1a8b: Difference between revisions
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<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=1a8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8b RCSB], [http://www.ebi.ac.uk/pdbsum/1a8b 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=1a8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8b RCSB], [http://www.ebi.ac.uk/pdbsum/1a8b PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ANXA5_RAT ANXA5_RAT]] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:11, 25 December 2014
RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINERAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE
Structural highlights
Function[ANXA5_RAT] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStructural evidence is presented for a 'Ca(2+)-bridging' mechanism, proposed for Ca(2+)-binding interfacial membrane proteins such as annexins, protein kinase C, and certain coagulation proteins. Crystal structures of Ca(2+)-annexin V complexes with phospholipid polar heads provide molecular details of 'Ca(2+)-bridges' as key features in the membrane attachment exhibited by these proteins. Distinct binding sites for phospholipid head groups are observed, including a novel, double-Ca2+ recognition site for phosphoserine that may serve as a phosphatidylserine receptor site in vivo. Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V.,Swairjo MA, Concha NO, Kaetzel MA, Dedman JR, Seaton BA Nat Struct Biol. 1995 Nov;2(11):968-74. PMID:7583670[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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