1a4p: Difference between revisions
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'''P11 (S100A10), LIGAND OF ANNEXIN II''' | {{Structure | ||
|PDB= 1a4p |SIZE=350|CAPTION= <scene name='initialview01'>1a4p</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''P11 (S100A10), LIGAND OF ANNEXIN II''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A4P is a [ | 1A4P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4P OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9886297 9886297] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s100 family]] | [[Category: s100 family]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:51 2008'' | ||
Revision as of 07:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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