2kbm

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Current revision (06:45, 1 May 2024) (edit) (undo)
 
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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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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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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<table><tr><td colspan='2'>[[2kbm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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">Solution NMR</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='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='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'>[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>
<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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[[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.
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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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cannon, B R]]
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[[Category: Rattus norvegicus]]
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[[Category: Morgan, M]]
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[[Category: Cannon BR]]
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[[Category: Varney, K M]]
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[[Category: Morgan M]]
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[[Category: Weber, D J]]
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[[Category: Varney KM]]
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[[Category: Wright, N T]]
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[[Category: Weber DJ]]
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[[Category: Acetylation]]
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[[Category: Wright NT]]
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[[Category: Actin capping]]
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[[Category: Actin-binding]]
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[[Category: Calcium]]
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[[Category: Capz]]
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[[Category: Conformational change]]
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[[Category: Cytoplasm]]
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[[Category: Ef-hand]]
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[[Category: Metal binding protein]]
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[[Category: Metal-binding]]
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[[Category: Protein-protein interaction]]
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[[Category: S100]]
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[[Category: Zinc]]
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Current revision

Ca-S100A1 interacting with TRTK12

PDB ID 2kbm

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