View source for 4cfq


==Ca-bound truncated (delta13C) and C3S, C81S and C86S mutated S100A4 complexed with non-muscle myosin IIA==
<StructureSection load='4cfq' size='340' side='right'caption='[[4cfq]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cfq]] 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=4CFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CFQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4cfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfq OCA], [https://pdbe.org/4cfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cfq RCSB], [https://www.ebi.ac.uk/pdbsum/4cfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S10A4_HUMAN S10A4_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
S100A4 interacts with many binding partners upon Ca2+ activation and is strongly associated with increased metastasis formation. In order to understand the role of the C-terminal random coil for the protein function we examined how small angle X-ray scattering of the wild-type S100A4 and its C-terminal deletion mutant (residues 1-88, Delta13) changes upon Ca2+ binding. We found that the scattering intensity of wild-type S100A4 changes substantially in the 0.15-0.25 A-1 q-range whereas a similar change is not visible in the C-terminus deleted mutant. Ensemble optimization SAXS modeling indicates that the entire C-terminus is extended when Ca2+ is bound. Pulsed field gradient NMR measurements provide further support as the hydrodynamic radius in the wild-type protein increases upon Ca2+ binding while the radius of Delta13 mutant does not change. Molecular dynamics simulations provide a rational explanation of the structural transition: the positively charged C-terminal residues associate with the negatively charged residues of the Ca2+-free EF-hands and these interactions loosen up considerably upon Ca2+-binding. As a consequence the Delta13 mutant has increased Ca2+ affinity and is constantly loaded at Ca2+ concentration ranges typically present in cells. The activation of the entire C-terminal random coil may play a role in mediating interaction with selected partner proteins of S100A4.

The C-Terminal Random Coil Region Tunes the Ca2+-Binding Affinity of S100A4 through Conformational Activation.,Duelli A, Kiss B, Lundholm I, Bodor A, Petoukhov MV, Svergun DI, Nyitray L, Katona G PLoS One. 2014 May 15;9(5):e97654. doi: 10.1371/journal.pone.0097654. eCollection, 2014. PMID:24830809<ref>PMID:24830809</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cfq" style="background-color:#fffaf0;"></div>

==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bodor A]]
[[Category: Duelli A]]
[[Category: Katona G]]
[[Category: Kiss B]]
[[Category: Lundholm I]]
[[Category: Nyitray L]]
[[Category: Petoukhov M]]
[[Category: Radnai L]]
[[Category: Svergun D]]