6U39

2.4 Angstrom crystal structure of the D129G Ca-CaM:CaV1.2 IQ domain complex

Summary for 6U39

• Entry DOI: 10.2210/pdb6u39/pdb
• Descriptor: Calmodulin-1, Voltage-dependent L-type calcium channel subunit alpha-1C, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: membrane protein, calcium-binding protein-membrane protein complex, calcium-binding protein/membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 20
• Total formula weight: 210985.06

Authors

Wang, K.,Van Petegem, F. (deposition date: 2019-08-21, release date: 2020-02-19, Last modification date: 2023-10-11)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)