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S100‐ANNEXIN COMPLEXES: SOME INSIGHTS FROM STRUCTURAL STUDIES
Author(s) -
LewitBentley Anita,
Réty Stéphane,
Sopkovade Oliveira Santos Jana,
Gerke Volker
Publication year - 2000
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.2000.0629
Subject(s) - annexin , annexin a2 , annexin a1 , chemistry , n terminus , calcium binding protein , fusion protein , biophysics , crystallography , calcium , microbiology and biotechnology , biochemistry , peptide sequence , biology , apoptosis , gene , organic chemistry , recombinant dna
Abstract 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 p11 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 p11 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.