title: An open or closed case for the conformation of calponin homology domains on F-actin?
abstract: Calponin homology domains link many different proteins to the surface of actin filaments. However, details of the structural interactions involved and the methods used to determine them are controversial. In the case of the actin-binding protein utrophin, for example, several models have been proposed for the binding of utrophin's calponin homology domains to actin. We review and evaluate these models and their supporting data.
authors.affiliation: Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA. wlehman@bu.edu
authors.forename: William
authors.initials: W
authors.lastname: Lehman
authors.forename: Roger
authors.initials: R
authors.lastname: Craig
authors.forename: John
authors.initials: J
authors.lastname: Kendrick-Jones
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Sutherland-Smith
mesh_terms: D000199:Actins / Q000737:chemistry*; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008840:Microfilament Proteins; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary / Q000502:physiology; D049411:Utrophin / Q000737:chemistry*; D000096985:Calponins
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D049411:Utrophin; D000096985:Calponins