1mux
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1mux.png|left|200px]] | ||
- | < | + | ==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES== |
- | + | <StructureSection load='1mux' size='340' side='right'caption='[[1mux]]' scene=''> | |
- | You may | + | == Structural highlights == |
- | or the | + | <table><tr><td colspan='2'>[[1mux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUX FirstGlance]. <br> |
- | or | + | </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='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=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</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=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [https://pdbe.org/1mux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB], [https://www.ebi.ac.uk/pdbsum/1mux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mux ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mux_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mux ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition. | ||
- | + | Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.,Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M J Mol Biol. 1998 Feb 13;276(1):165-76. PMID:9514729<ref>PMID:9514729</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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- | == | + | |
- | < | + | |
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
- | [[Category: Furuya | + | [[Category: Furuya T]] |
- | [[Category: Ikura | + | [[Category: Ikura M]] |
- | [[Category: Mase | + | [[Category: Mase T]] |
- | [[Category: Osawa | + | [[Category: Osawa M]] |
- | [[Category: Swindells | + | [[Category: Swindells MB]] |
- | [[Category: Tanaka | + | [[Category: Tanaka T]] |
- | [[Category: Tanikawa | + | [[Category: Tanikawa J]] |
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Current revision
SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES
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Categories: Large Structures | Xenopus laevis | Furuya T | Ikura M | Mase T | Osawa M | Swindells MB | Tanaka T | Tanikawa J