title: Conformational changes of actin induced by calponin.
abstract: Calponin, an actin-linked regulatory protein in smooth muscle, caused a remarkable change in the fluorescence intensity of pyrene-labeled actin in the filamentous form. Calponin, an equimolar ratio to actin, decreased the fluorescence intensity of pyrene-labeled F-actin by some 60% to the level near monomeric actin. This change was partially reversed by Ca2+, when calmodulin was present. Thus it appears that calponin causes conformational changes in actin molecules in an actin filament so as to inhibit their interactions with myosin.
authors.affiliation: Department of Biology, Faculty of Science, Chiba University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Noda
authors.forename: M
authors.initials: M
authors.lastname: Ito
authors.forename: S
authors.initials: S
authors.lastname: Watanabe
authors.forename: K
authors.initials: K
authors.lastname: Takahashi
authors.forename: K
authors.initials: K
authors.lastname: Maruyama
mesh_terms: D000199:Actins / Q000187:drug effects*; D000818:Animals; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D002645:Chickens; D004305:Dose-Response Relationship, Drug; D008840:Microfilament Proteins; D009124:Muscle Proteins / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects; D000096985:Calponins
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D000096985:Calponins