Download MendeleyCa(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V.
Swairjo, M.A., Concha, N.O., Kaetzel, M.A., Dedman, J.R., Seaton, B.A.(1995) Nat Struct Biol 2: 968-974
- PubMed: 7583670
- DOI: https://doi.org/10.1038/nsb1195-968
- Primary Citation of Related Structures:
1A8A, 1A8B - PubMed 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.
Organizational Affiliation:
Department of Physiology, Boston University School of Medicine, Massachusetts 02118, USA.
