2kbm

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==Ca-S100A1 interacting with TRTK12==
==Ca-S100A1 interacting with TRTK12==
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<StructureSection load='2kbm' size='340' side='right' caption='[[2kbm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2kbm' size='340' side='right'caption='[[2kbm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2kbm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KBM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2kbm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KBM FirstGlance]. <br>
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</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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k2f|2k2f]], [[1zfs|1zfs]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2k2f|2k2f]], [[1zfs|1zfs]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Capza2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), S100a1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Capza2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), S100a1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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<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=2kbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kbm OCA], [http://pdbe.org/2kbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kbm RCSB], [http://www.ebi.ac.uk/pdbsum/2kbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kbm ProSAT]</span></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=2kbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kbm OCA], [https://pdbe.org/2kbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kbm RCSB], [https://www.ebi.ac.uk/pdbsum/2kbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kbm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAZA2_RAT CAZA2_RAT]] 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 (By similarity). [[http://www.uniprot.org/uniprot/S10A1_RAT S10A1_RAT]] 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.
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[[https://www.uniprot.org/uniprot/CAZA2_RAT CAZA2_RAT]] 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 (By similarity). [[https://www.uniprot.org/uniprot/S10A1_RAT S10A1_RAT]] 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[F-actin capping protein|F-actin capping protein]]
*[[F-actin capping protein|F-actin capping protein]]
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*[[S100 protein|S100 protein]]
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Buffalo rat]]
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[[Category: Large Structures]]
[[Category: Cannon, B R]]
[[Category: Cannon, B R]]
[[Category: Morgan, M]]
[[Category: Morgan, M]]

Revision as of 08:15, 7 April 2021

Ca-S100A1 interacting with TRTK12

PDB ID 2kbm

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