title: Structure of the regulatory domain of scallop myosin at 2.8 A resolution.
abstract: The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.
authors.affiliation: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.
authors.forename: X
authors.initials: X
authors.lastname: Xie
authors.forename: D H
authors.initials: DH
authors.lastname: Harrison
authors.forename: I
authors.initials: I
authors.lastname: Schlichting
authors.forename: R M
authors.initials: RM
authors.lastname: Sweet
authors.forename: V N
authors.initials: VN
authors.lastname: Kalabokis
authors.forename: A G
authors.initials: AG
authors.lastname: Szent-Györgyi
authors.forename: C
authors.initials: C
authors.lastname: Cohen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D008974:Mollusca; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D009218:Myosins; D002118:Calcium