1a4p

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<StructureSection load='1a4p' size='340' side='right'caption='[[1a4p]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='1a4p' size='340' side='right'caption='[[1a4p]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1a4p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1a4p]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4P FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4p OCA], [https://pdbe.org/1a4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4p RCSB], [https://www.ebi.ac.uk/pdbsum/1a4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4p ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4p OCA], [https://pdbe.org/1a4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4p RCSB], [https://www.ebi.ac.uk/pdbsum/1a4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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.
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[https://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a4p ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a4p ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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<ref>PMID:9886297</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1a4p" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gerke, V]]
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[[Category: Gerke V]]
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[[Category: Lewit-Bentley, A]]
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[[Category: Lewit-Bentley A]]
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[[Category: Osterloh, D]]
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[[Category: Osterloh D]]
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[[Category: Renouard, M]]
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[[Category: Renouard M]]
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[[Category: Rety, S]]
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[[Category: Rety S]]
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[[Category: Russo-Marie, F]]
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[[Category: Russo-Marie F]]
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[[Category: Sopkova, J]]
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[[Category: Sopkova J]]
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[[Category: Calcium-phospholipid binding protein complex]]
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[[Category: Calcium/phospholipid binding protein]]
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[[Category: Ef-hand protein]]
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[[Category: Ligand of annexin ii]]
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[[Category: S100 family]]
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Revision as of 15:21, 13 March 2024

P11 (S100A10), LIGAND OF ANNEXIN II

PDB ID 1a4p

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