Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology Life Sciences Institute University of British Columbia V6T 1Z3 Vancouver BC Canada
2. Department of Chemistry and Bioscience Aalborg University Aalborg Denmark
Funder
Canadian Institutes of Health Research
Det Frie Forskningsråd
Lundbeckfonden
Novo Nordisk
Publisher
Wiley
Subject
Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1113/JP279307
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1. PHENIX: a comprehensive Python-based system for macromolecular structure solution
2. Engineered calmodulins reveal the unexpected eminence of Ca2+ channel inactivation in controlling heart excitation
3. Thermodynamics of Calcium binding to the Calmodulin N-terminal domain to evaluate site-specific affinity constants and cooperativity
4. Dynamic switching of calmodulin interactions underlies Ca2+ regulation of CaV1.3 channels
5. Calmodulin regulation (calmodulation) of voltage-gated calcium channels
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