RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE

File:1a8b.gif


1a8b, resolution 1.9Å

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OverviewOverview

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.

About this StructureAbout this Structure

1A8B is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

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