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Article

Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin.

Biochemistry - 28 Feb 1995

Miller C J, Reisler E

Abstract excerpt

Yeast actin mutants with alanines replacing charged amino acid pairs D24/D25, E99/E100, D80/D81, and E83/K84 were studied to assess their role in interactions with myosin. In a previous report Dictyostelium actin filaments with residues D24/D25 or E99/E100 replaced with histidines showed complete or partial loss of filament sliding in the in vitro motility assay [Johara, M., et al. (1993) Proc. Natl. Acad. Sci....

Topics

Actins
Adenosine Triphosphate
Amino Acids
Animals
Binding Sites
Enzyme Activation
In Vitro Techniques
Molecular Structure
Mutagenesis
Mutation
Myosins
Polymers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Rabbits

Saccharomyces cerevisiae

Source

Identifiers

PMID: 7873552
DOI: 10.1021/bi00008a037

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7873552-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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