Article
A conserved negatively charged amino acid modulates function in human nonmuscle myosin IIA.
Biochemistry - 9 May 2000
Wang F, Harvey E V, Conti M A, Wei D, Sellers J R
Abstract excerpt
A myosin surface loop (amino acids 391-404) is postulated to be an important actin binding site. In human beta-cardiac myosin, mutation of arginine-403 to a glutamine or a tryptophan causes hypertrophic cardiomyopathy. There is a phosphorylatable serine or threonine residue present on this loop in some lower eukaryotic myosin class I and myosin class VI molecules. Phosphorylation of the myosin I molecules at this...
Topics
- Actins
- Amino Acid Sequence
- Baculoviridae
- Ca(2+) Mg(2+)-ATPase
- Cardiomyopathy, Hypertrophic
- Humans
- Kinetics
- Models, Molecular
- Molecular Motor Proteins
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Myosin Subfragments
- Myosins
- Protein Binding
- Recombinant Proteins
- Sequence Alignment
- Static Electricity