1CKK

CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT

Summary for 1CKK

• Entry DOI: 10.2210/pdb1ckk/pdb
• Descriptor: Calmodulin-1, Calcium/calmodulin-dependent protein kinase kinase 1, CALCIUM ION (3 entities in total)
• Functional Keywords: complex (calmodulin-peptide), calmodulin, camkk, calmodulin-peptide complex
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 2
• Total formula weight: 19905.36

Authors

Osawa, M.,Tokumitsu, H.,Swindells, M.B.,Kurihara, H.,Orita, M.,Shibanuma, T.,Furuya, T.,Ikura, M. (deposition date: 1998-11-20, release date: 1999-09-10, Last modification date: 2023-12-27)

Primary citation

Osawa, M.,Tokumitsu, H.,Swindells, M.B.,Kurihara, H.,Orita, M.,Shibanuma, T.,Furuya, T.,Ikura, M.
A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase.
Nat.Struct.Biol., 6:819-824, 1999

PubMed Abstract: 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.

PubMed: 10467092
DOI: 10.1038/12271

Experimental method

SOLUTION NMR