This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1mux
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1mux.gif|left|200px]] | [[Image:1mux.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1mux", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1mux| PDB=1mux | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES''' | '''SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES''' | ||
| Line 32: | Line 29: | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
[[Category: Tanikawa, J.]] | [[Category: Tanikawa, J.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding]] |
| - | [[Category: | + | [[Category: Calmodulin]] |
| - | [[Category: | + | [[Category: Naphthalenesulfonamide]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: W-7]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:45:08 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:45, 2 May 2008
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 Page seeded by OCA on Sat May 3 01:45:08 2008
Categories: Single protein | Xenopus laevis | Furuya, T. | Ikura, M. | Mase, T. | Osawa, M. | Swindells, M B. | Tanaka, T. | Tanikawa, J. | Calcium-binding | Calmodulin | Naphthalenesulfonamide | Nmr | W-7
