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 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.
Swairjo
M A
MA
Department of Physiology, Boston University School of Medicine, Massachusetts 02118, USA.
Concha
N O
NO
Kaetzel
M A
MA
Dedman
J R
JR
Seaton
B A
BA
D000595:Amino Acid Sequence; D017304:Annexin A5 / Q000737:chemistry* / Q000378:metabolism; D017302:Annexins; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010714:Phosphatidylethanolamines / Q000737:chemistry / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry* / Q000378:metabolism; D010768:Phosphoserine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding
D017304:Annexin A5; D017302:Annexins; D010714:Phosphatidylethanolamines; D010743:Phospholipids; C002449:glycerophosphoethanolamine; D010768:Phosphoserine; C067651:glycerophosphoserine; D002118:Calcium