1CKK

CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT

1CKK の概要

• エントリーDOI: 10.2210/pdb1ckk/pdb
• 分子名称: Calmodulin-1, Calcium/calmodulin-dependent protein kinase kinase 1, CALCIUM ION (3 entities in total)
• 機能のキーワード: complex (calmodulin-peptide), calmodulin, camkk, calmodulin-peptide complex
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19905.36

構造登録者

Osawa, M.,Tokumitsu, H.,Swindells, M.B.,Kurihara, H.,Orita, M.,Shibanuma, T.,Furuya, T.,Ikura, M. (登録日: 1998-11-20, 公開日: 1999-09-10, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

SOLUTION NMR