1a4p
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(New page: 200px<br /> <applet load="1a4p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4p, resolution 2.25Å" /> '''P11 (S100A10), LIGA...)
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Revision as of 13:49, 12 November 2007
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P11 (S100A10), LIGAND OF ANNEXIN II
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.
About this Structure
1A4P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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