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==Ca-bound S100A4 C3S, C81S, C86S and F45W mutant complexed with non- muscle myosin IIA==
==Ca-bound S100A4 C3S, C81S, C86S and F45W mutant complexed with non- muscle myosin IIA==
<StructureSection load='4cfr' size='340' side='right' caption='[[4cfr]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4cfr' size='340' side='right'caption='[[4cfr]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cfr]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CFR FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cfr]] is a 3 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=4CFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CFR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cfq|4cfq]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cfr RCSB], [http://www.ebi.ac.uk/pdbsum/4cfr PDBsum]</span></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=4cfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cfr OCA], [https://pdbe.org/4cfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cfr RCSB], [https://www.ebi.ac.uk/pdbsum/4cfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cfr ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/MYH9_HUMAN MYH9_HUMAN]] MYH9-related thrombocytopenia;Autosomal dominant nonsyndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9-related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures.  Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD).
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYH9_HUMAN MYH9_HUMAN]] Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10.<ref>PMID:20052411</ref> 
[https://www.uniprot.org/uniprot/S10A4_HUMAN S10A4_HUMAN]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4cfr" style="background-color:#fffaf0;"></div>
==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bodor, A]]
[[Category: Homo sapiens]]
[[Category: Duelli, A]]
[[Category: Large Structures]]
[[Category: Katona, G]]
[[Category: Bodor A]]
[[Category: Kiss, B]]
[[Category: Duelli A]]
[[Category: Lundholm, I]]
[[Category: Katona G]]
[[Category: Nyitray, L]]
[[Category: Kiss B]]
[[Category: Petoukhov, M]]
[[Category: Lundholm I]]
[[Category: Radnai, L]]
[[Category: Nyitray L]]
[[Category: Svergun, D]]
[[Category: Petoukhov M]]
[[Category: Ca-binding]]
[[Category: Radnai L]]
[[Category: Ca-binding protein-motor protein complex]]
[[Category: Svergun D]]
[[Category: Ef-hand]]
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