4hex
From Proteopedia
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| - | [[Image:4hex.jpg|left|200px]] | ||
| - | + | ==A novel conformation of calmodulin== | |
| + | <StructureSection load='4hex' size='340' side='right'caption='[[4hex]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEX 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]] 2.001Å</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [https://pdbe.org/4hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [https://www.ebi.ac.uk/pdbsum/4hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] 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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23] | ||
| - | == | + | ==See Also== |
| - | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Chichili | + | [[Category: Chichili VPR]] |
| - | [[Category: Kumar | + | [[Category: Kumar V]] |
| - | [[Category: Sivaraman | + | [[Category: Sivaraman J]] |
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Current revision
A novel conformation of calmodulin
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