Abstract
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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Annexin A5 / chemistry*
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Annexin A5 / metabolism
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Annexins
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Calcium / chemistry*
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Calcium / metabolism
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Membranes / metabolism
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Models, Molecular
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Molecular Sequence Data
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Phosphatidylethanolamines / chemistry
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Phosphatidylethanolamines / metabolism
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Phospholipids / chemistry*
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Phospholipids / metabolism
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Phosphoserine / analogs & derivatives
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Phosphoserine / chemistry
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Phosphoserine / metabolism
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Protein Binding
Substances
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Annexin A5
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Annexins
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Phosphatidylethanolamines
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Phospholipids
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glycerophosphoethanolamine
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Phosphoserine
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glycerophosphoserine
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Calcium