S100-annexin complexes:: Some insights from structural studies

被引:51
作者
Lewit-Bentley, A
Réty, S
Sopkova-de Oliveira Santos, J
Gerke, V
机构
[1] Ctr Univ Paris Sud, Utilisat Rayonnement Electromagnet Lab, CNRS, CEA,MENRT, F-91898 Orsay, France
[2] Univ Munster, Inst Med Biochem, ZMBE, D-48149 Munster, Germany
关键词
calcium-binding proteins; protein-peptide complex; crystal structure; membrane-protein interactions;
D O I
10.1006/cbir.2000.0629
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Several annexins have been shown to bind proteins that belong to the S100 calcium-binding protein family. The two best-characterized complexes are annexin II with pll and annexin I with S100C, the former of which has been implicated in membrane fusion processes. We have solved the crystal structures of the complexes of pll with annexin II N-terminus and of S100C with annexin I N-terminus. Using these structural results,as well as electron microscopy observations of liposome junctions formed in the presence of such complexes (Lambert et al., 1997 J Mol Biol 272, 42-55), we propose a computer generated model for the entire annexin II/p11 complex. (C) 2000 Academic Press.
引用
收藏
页码:799 / 802
页数:4
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