6U3D

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

Summary for 6U3D

Entry DOI	10.2210/pdb6u3d/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	4
Total formula weight	42399.37
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation