8b6q
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==X-ray structure of the haloalkane dehalogenase HaloTag7 with an insertion of Calmodulin-M13 fusion at position 154-156 that mimic the structure of CaProLa, an calcium gated protein labeling technology== | |
- | + | <StructureSection load='8b6q' size='340' side='right'caption='[[8b6q]], [[Resolution|resolution]] 2.60Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8b6q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rhodococcus_sp. Rhodococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B6Q 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]] 2.6Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8b6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b6q OCA], [https://pdbe.org/8b6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b6q RCSB], [https://www.ebi.ac.uk/pdbsum/8b6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b6q ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14. | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref> [https://www.uniprot.org/uniprot/DHAA_RHOSO DHAA_RHOSO] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Rhodococcus sp]] | ||
+ | [[Category: Hiblot J]] | ||
+ | [[Category: Johnsson K]] | ||
+ | [[Category: Tarnawski M]] |
Current revision
X-ray structure of the haloalkane dehalogenase HaloTag7 with an insertion of Calmodulin-M13 fusion at position 154-156 that mimic the structure of CaProLa, an calcium gated protein labeling technology
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