Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I.
Recent studies have revealed that binding of annexin I to phospholipids induces the formation of a second phospholipid binding site. It is shown that the N terminus on the concave side of membrane-bound annexin I is cleaved much faster by trypsin or cathepsin than the N terminus of the free protein. The reactivity of the unique disulfide bond located near the concave face was similarly increased by membrane binding. These results demonstrate that Ca(2+)-dependent membrane binding induces a conformational change on the concave side of the annexin I molecule and support the notion that this face of the molecule may contribute to the formation of the secondary membrane-binding site.
de la Fuente
M
M
Departamento de Fislología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiago, Chile. mdelafue@machi.med.uchile.cl
Ossa
C G
CG
D017305:Annexin A1 / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002122:Calcium Chloride / Q000494:pharmacology; D007700:Kinetics; D008081:Liposomes; D010714:Phosphatidylethanolamines; D010718:Phosphatidylserines; D011487:Protein Conformation / Q000187:drug effects; D014357:Trypsin / Q000378:metabolism
D017305:Annexin A1; D008081:Liposomes; D010714:Phosphatidylethanolamines; D010718:Phosphatidylserines; D014357:Trypsin; D002122:Calcium Chloride