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==Ca2+-S100B-TRTK-12 complex==
==Ca2+-S100B-TRTK-12 complex==
<StructureSection load='1mq1' size='340' side='right' caption='[[1mq1]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
<StructureSection load='1mq1' size='340' side='right'caption='[[1mq1]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mq1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MQ1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mq1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQ1 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uwo|1uwo]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq1 OCA], [https://pdbe.org/1mq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq1 ProSAT]</span></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=1mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq1 OCA], [http://pdbe.org/1mq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mq1 RCSB], [http://www.ebi.ac.uk/pdbsum/1mq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/S100B_HUMAN S100B_HUMAN]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:20351179</ref> [[http://www.uniprot.org/uniprot/CAZA1_HUMAN CAZA1_HUMAN]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
[https://www.uniprot.org/uniprot/S100B_HUMAN S100B_HUMAN] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:20351179</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1mq1" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1mq1" style="background-color:#fffaf0;"></div>
==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: McClintock, K A]]
[[Category: Large Structures]]
[[Category: Shaw, G S]]
[[Category: McClintock KA]]
[[Category: Ef-hand]]
[[Category: Shaw GS]]
[[Category: Metal binding protein]]
[[Category: Protein-peptide complex]]
Retrieved from "https://proteopedia.org/1mq1"