1ckk
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| Ligands: | |||||||
| Gene: | XENOPUS LAEVIS (Xenopus laevis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT
OverviewOverview
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 StructureAbout this Structure
1CKK is a Single protein structure of sequence from Rattus norvegicus and Xenopus laevis. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun Mar 30 19:23:24 2008