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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...

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Identifiers

PMID: 10820029
DOI: 10.1021/bi000133x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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