Opening of tandem calponin homology domains regulates their affinity for F-actin.
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ABSTRACT:
SUBMITTER: Galkin VE
PROVIDER: S-EPMC2921939 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Publications
Opening of tandem calponin homology domains regulates their affinity for F-actin.
Galkin Vitold E VE Orlova Albina A Salmazo Anita A Djinovic-Carugo Kristina K Egelman Edward H EH
Nature structural & molecular biology 20100411 5
Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and ...[more]
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