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1ckk
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(New page: 200px<br /><applet load="1ckk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ckk" /> '''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PRO...)
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Revision as of 10:25, 20 November 2007
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CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT
Overview
The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a, 26-residue peptide, corresponding to the CaM-binding domain of rat, Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by, NMR spectroscopy. In this complex, the CaMKK peptide forms a fold, comprising an alpha-helix and a hairpin-like loop whose C-terminus folds, back on itself. The binding orientation of this CaMKK peptide by the two, CaM domains is opposite to that observed in all other CaM-target complexes, determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM, anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This, 14-residue separation between two key hydrophobic groups is also unique, among previously determined CaM complexes. The present structure, represents a new and distinct class of Ca2+/CaM target recognition that, may be shared by other Ca2+/CaM-stimulated proteins.
About this Structure
1CKK is a Single protein structure of sequence from Rattus norvegicus and Xenopus laevis with CA as ligand. Full crystallographic information is available from OCA.
Reference
A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase., Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M, Nat Struct Biol. 1999 Sep;6(9):819-24. PMID:10467092
Page seeded by OCA on Tue Nov 20 12:32:14 2007
