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1a4p

From Proteopedia

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{{STRUCTURE_1a4p| PDB=1a4p | SCENE= }}
{{STRUCTURE_1a4p| PDB=1a4p | SCENE= }}
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'''P11 (S100A10), LIGAND OF ANNEXIN II'''
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===P11 (S100A10), LIGAND OF ANNEXIN II===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9886297 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9886297}}
==About this Structure==
==About this Structure==
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[[Category: Ligand of annexin ii]]
[[Category: Ligand of annexin ii]]
[[Category: S100 family]]
[[Category: S100 family]]
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Revision as of 13:07, 30 June 2008

Image:1a4p.png

Template:STRUCTURE 1a4p

P11 (S100A10), LIGAND OF ANNEXIN II

Template:ABSTRACT PUBMED 9886297

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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