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4drw

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Current revision (14:43, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4drw]] is a 6 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=4DRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRW FirstGlance]. <br>
<table><tr><td colspan='2'>[[4drw]] is a 6 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=4DRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRW 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=4drw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drw OCA], [https://pdbe.org/4drw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drw RCSB], [https://www.ebi.ac.uk/pdbsum/4drw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drw 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]] 3.5&#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=4drw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drw OCA], [https://pdbe.org/4drw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drw RCSB], [https://www.ebi.ac.uk/pdbsum/4drw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drw 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.[[https://www.uniprot.org/uniprot/ANXA2_HUMAN ANXA2_HUMAN]] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.
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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.[https://www.uniprot.org/uniprot/ANXA2_HUMAN ANXA2_HUMAN] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plasma membrane repair involves the coordinated effort of proteins and the inner phospholipid surface to mend the rupture and return the cell back to homeostasis. Here, we present the three-dimensional structure of a multiprotein complex that includes S100A10, annexin A2, and AHNAK, which along with dysferlin, functions in muscle and cardiac tissue repair. The 3.5 A resolution X-ray structure shows that a single region from the AHNAK C terminus is recruited by an S100A10-annexin A2 heterotetramer, forming an asymmetric ternary complex. The AHNAK peptide adopts a coil conformation that arches across the heterotetramer contacting both annexin A2 and S100A10 protomers with tight affinity ( approximately 30 nM) and establishing a structural rationale whereby both S100A10 and annexin proteins are needed in AHNAK recruitment. The structure evokes a model whereby AHNAK is targeted to the membrane surface through sandwiching of the binding region between the S100A10/annexin A2 complex and the phospholipid membrane.
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Structure of an asymmetric ternary protein complex provides insight for membrane interaction.,Dempsey BR, Rezvanpour A, Lee TW, Barber KR, Junop MS, Shaw GS Structure. 2012 Oct 10;20(10):1737-45. doi: 10.1016/j.str.2012.08.004. Epub 2012 , Aug 30. PMID:22940583<ref>PMID:22940583</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 4drw" style="background-color:#fffaf0;"></div>
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==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__
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</StructureSection>
</StructureSection>

Current revision

Crystal Structure of the Ternary Complex between S100A10, an Annexin A2 N-terminal Peptide and an AHNAK Peptide

PDB ID 4drw

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