1mux
From Proteopedia
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|PDB= 1mux |SIZE=350|CAPTION= <scene name='initialview01'>1mux</scene> | |PDB= 1mux |SIZE=350|CAPTION= <scene name='initialview01'>1mux</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=WW7:N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE'>WW7</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
[[Category: Tanikawa, J.]] | [[Category: Tanikawa, J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: WW7]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: calmodulin]] | [[Category: calmodulin]] | ||
| Line 38: | Line 39: | ||
[[Category: w-7]] | [[Category: w-7]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:28 2008'' |
Revision as of 19:21, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES
Overview
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.
About this Structure
1MUX is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
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
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