6U3D

1.75 Angstrom crystal structure of the N53I Ca-CaM:CaV1.2 IQ domain complex

6U3D の概要

• エントリーDOI: 10.2210/pdb6u3d/pdb
• 分子名称: Calmodulin-1, Voltage-dependent L-type calcium channel subunit alpha-1C, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, calcium-binding protein-membrane protein complex, calcium-binding protein/membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 42399.37

構造登録者

Wang, K.,Van Petegem, F. (登録日: 2019-08-21, 公開日: 2020-02-19, 最終更新日: 2023-10-11)

主引用文献

Wang, K.,Brohus, M.,Holt, C.,Overgaard, M.T.,Wimmer, R.,Van Petegem, F.
Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding.
J. Physiol. (Lond.), 598:1169-1186, 2020

PubMed Abstract: Mutations in the calmodulin protein (CaM) are associated with arrhythmia syndromes. This study focuses on understanding the structural characteristics of CaM disease mutants and their interactions with the voltage-gated calcium channel Ca 1.2. Arrhythmia mutations in CaM can lead to loss of Ca binding, uncoupling of Ca binding cooperativity, misfolding of the EF-hands and altered affinity for the calcium channel. These results help us to understand how different CaM mutants have distinct effects on structure and interactions with protein targets to cause disease.

PubMed: 32012279
DOI: 10.1113/JP279307

実験手法

X-RAY DIFFRACTION (1.75 Å)