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1a4p

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Revision as of 17:05, 25 December 2014

P11 (S100A10), LIGAND OF ANNEXIN II

Structural highlights

1a4p is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[S10AA_HUMAN] Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A. The crystal structure of a complex of p11 with the annexin II N-terminal peptide. Nat Struct Biol. 1999 Jan;6(1):89-95. PMID:9886297 doi:10.1038/4965

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a4p"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a4p RCSB], [http://www.ebi.ac.uk/pdbsum/1a4p PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/S10AA_HUMAN S10AA_HUMAN]] Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1a4p

From Proteopedia

Revision as of 17:05, 25 December 2014

P11 (S100A10), LIGAND OF ANNEXIN II

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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