CA2+-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 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.