Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V

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 molecul...

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Veröffentlicht in:Nature structural biology 1995-11, Vol.2 (11), p.968-974
Hauptverfasser: Swairjo, M A, Concha, N O, Kaetzel, M A, Dedman, J R, Seaton, B A
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container_end_page 974
container_issue 11
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container_title Nature structural biology
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creator Swairjo, M A
Concha, N O
Kaetzel, M A
Dedman, J R
Seaton, B A
description 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.
doi_str_mv 10.1038/nsb1195-968
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subjects Amino Acid Sequence
Annexin A5 - chemistry
Annexin A5 - metabolism
Annexins
Calcium - chemistry
Calcium - metabolism
Membranes - metabolism
Models, Molecular
Molecular Sequence Data
Phosphatidylethanolamines - chemistry
Phosphatidylethanolamines - metabolism
Phospholipids - chemistry
Phospholipids - metabolism
Phosphoserine - analogs & derivatives
Phosphoserine - chemistry
Phosphoserine - metabolism
Protein Binding
title Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
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