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Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V

Nature Structural Biology volume 2, pages 968–974 (1995)Cite this article

Abstract

Structural evidence is presented for a ‘Ca2+-bridging’ mechanism, proposed for Ca2+- binding interfacial membrane proteins such as annexins, protein kinase C, and certain coagulation proteins. Crystal structures of Ca2+-annexin V complexes with phospholipid polar heads provide molecular details of ‘Ca2+-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.

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Author notes

  1. N.O. Concha

    Present address: Center for Advanced Research in Biotechnology, University of Maryland, Rockville, Maryland, 20850, USA

Authors and Affiliations

  1. Structural Biology Group, Department of Physiology, Boston University School of Medicine, 80 East Concord Street, Boston, Massachusetts, 02118, USA

    M.A. Swairjo, N.O. Concha & B.A. Seaton

  2. Department of Molecular and Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, Ohio, 45267, USA

    M.A. Kaetzel & J.R. Dedman

Authors
  1. M.A. Swairjo
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  2. N.O. Concha
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  3. M.A. Kaetzel
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  4. J.R. Dedman
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  5. B.A. Seaton
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Swairjo, M., Concha, N., Kaetzel, M. et al. Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat Struct Mol Biol 2, 968–974 (1995). https://doi.org/10.1038/nsb1195-968

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