The crystal structure of a complex of p11 with the annexin II N-terminal peptide.
The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.
Réty
S
S
LURE (CNRS, CEA, MENRT), Centre Universitaire Paris-Sud, Orsay, France.
Sopkova
J
J
Renouard
M
M
Osterloh
D
D
Gerke
V
V
Tabaries
S
S
Russo-Marie
F
F
Lewit-Bentley
A
A
D000818:Animals; D017306:Annexin A2 / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002118:Calcium; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D009418:S100 Proteins / Q000737:chemistry* / Q000378:metabolism
D017306:Annexin A2; D009418:S100 Proteins; D002118:Calcium