2K0E

A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction

2K0E の概要

• エントリーDOI: 10.2210/pdb2k0e/pdb
• 関連するPDBエントリー: 1J7O 1J7P 2K0F
• 分子名称: Calmodulin, CALCIUM ION (2 entities in total)
• 機能のキーワード: ef hands, ensemble, helix bundle, calcium binding, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle: P62158
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16881.66

構造登録者

Gsponer, J.,Christodoulou, J.,Cavalli, A.,Bui, J.M.,Richter, B.,Dobson, C.M.,Vendruscolo, M. (登録日: 2008-02-02, 公開日: 2008-06-10, 最終更新日: 2024-05-29)

主引用文献

Gsponer, J.,Christodoulou, J.,Cavalli, A.,Bui, J.M.,Richter, B.,Dobson, C.M.,Vendruscolo, M.
A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction
Structure, 16:736-746, 2008

PubMed Abstract: We used nuclear magnetic resonance data to determine ensembles of conformations representing the structure and dynamics of calmodulin (CaM) in the calcium-bound state (Ca(2+)-CaM) and in the state bound to myosin light chain kinase (CaM-MLCK). These ensembles reveal that the Ca(2+)-CaM state includes a range of structures similar to those present when CaM is bound to MLCK. Detailed analysis of the ensembles demonstrates that correlated motions within the Ca(2+)-CaM state direct the structural fluctuations toward complex-like substates. This phenomenon enables initial ligation of MLCK at the C-terminal domain of CaM and induces a population shift among the substates accessible to the N-terminal domain, thus giving rise to the cooperativity associated with binding. Based on these results and the combination of modern free energy landscape theory with classical allostery models, we suggest that a coupled equilibrium shift mechanism controls the efficient binding of CaM to a wide range of ligands.

PubMed: 18462678
DOI: 10.1016/j.str.2008.02.017

実験手法

SOLUTION NMR