1a8a

RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOSERINE

spinqualitylabelsall models 1a8a, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a8a is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ACE, CA, GSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed Structural 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Annexin 3D structures

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