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Article

Structural rearrangements in the active site of smooth-muscle myosin.

Biophysical journal - 1 Sept 2005

Robertson C Ian, Gaffney Donald P, Chrin Lynn R, Berger Christopher L

Abstract excerpt

Structural rearrangements of the myosin upper-50 kD subdomain are thought to play a key role in coordinating actin binding with nucleotide hydrolysis during the myosin ATPase cycle. Such rearrangements could open and close the active site in opposition to the actin-binding cleft, helping explain the opposing affinities of myosin for actin and nucleotide. To directly examine conformational changes across the...

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Identifiers

PMID: 15951390
DOI: 10.1529/biophysj.105.059840
PMCID: PMC1366691

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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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