Interdomain Linker Determines Primarily the Structural Stability of Dystrophin and Utrophin Tandem Calponin-Homology Domains Rather than Their Actin-Binding Affinity
Author:
Affiliation:
1. Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, and ‡Program in Structural Biology and Biochemistry, University of Colorado Anschutz Medical Campus, Aurora, Colorado 80045, United States
Funder
BioFrontiers Institute, University of Colorado Boulder
American Heart Association
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00741
Reference46 articles.
1. Calponin homology domains at a glance
2. Novel structural insights into F-actin-binding and novel functions of calponin homology domains
3. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
4. Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer
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3. Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain;Frontiers in Cell and Developmental Biology;2020-05-14
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