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[[Image:1mux.gif|left|200px]]


{{Structure
==SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES==
|PDB= 1mux |SIZE=350|CAPTION= <scene name='initialview01'>1mux</scene>
<StructureSection load='1mux' size='340' side='right'caption='[[1mux]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene>
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mux OCA], [http://www.ebi.ac.uk/pdbsum/1mux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mux RCSB]</span>
== 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 NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mux" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1MUX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUX OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9514729 9514729]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Furuya, T.]]
[[Category: Furuya T]]
[[Category: Ikura, M.]]
[[Category: Ikura M]]
[[Category: Mase, T.]]
[[Category: Mase T]]
[[Category: Osawa, M.]]
[[Category: Osawa M]]
[[Category: Swindells, M B.]]
[[Category: Swindells MB]]
[[Category: Tanaka, T.]]
[[Category: Tanaka T]]
[[Category: Tanikawa, J.]]
[[Category: Tanikawa J]]
[[Category: calcium-binding]]
[[Category: calmodulin]]
[[Category: complex (calmodulin/inhibitor)]]
[[Category: naphthalenesulfonamide]]
[[Category: nmr]]
[[Category: w-7]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:28 2008''
Retrieved from "https://proteopedia.org/1mux"