CA2+-BRIDGING MECHANISM AND PHOSPHOLIPID HEAD GROUP RECOGNITION IN THE MEMBRANE-BINDING PROTEIN ANNEXIN-V

被引：284
作者：
SWAIRJO, MA
CONCHA, NO
KAETZEL, MA
DEDMAN, JR
SEATON, BA
机构：
[1] BOSTON UNIV,SCH MED,DEPT PHYSIOL,STRUCT BIOL GRP,BOSTON,MA 02118
[2] UNIV CINCINNATI,COLL MED,DEPT MOLEC & CELLULAR PHYSIOL,CINCINNATI,OH 45267
来源：
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 11期
关键词：
D O I：
10.1038/nsb1195-968
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：968 / 974
页数：7
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