Ontology highlight
ABSTRACT:
SUBMITTER: Broderick MJ
PROVIDER: S-EPMC3642092 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Broderick Mike J F MJ Bobkov Andrey A Winder Steve J SJ
FEBS open bio 20120121
Structural analyses of actin binding regions comprising tandem calponin homology domains alone and when bound to F-actin have revealed a number of different conformations with calponin homology domains in 'open' and 'closed' positions. In an attempt to resolve these issues we have examined the properties of the utrophin actin binding domain in open and closed conformations in order to verify the conformation when bound to F-actin. Locking the actin binding domain in a closed conformation using e ...[more]