1bt6: Difference between revisions

Revision as of 12:58, 21 February 2008

P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N-TERMINUS

OverviewOverview

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.

About this StructureAbout this Structure

1BT6 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of a complex of p11 with the annexin II N-terminal peptide., Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A, Nat Struct Biol. 1999 Jan;6(1):89-95. PMID:9886297

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: s100 family]]
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