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Article

Actin hydrophobic loop 262-274 and filament nucleation and elongation.

Journal of molecular biology - 18 Jan 2008

Shvetsov Alexander, Galkin Vitold E, Orlova Albina, Phillips Martin, Bergeron Sarah E, Rubenstein Peter A, Egelman Edward H, Reisler Emil

Abstract excerpt

The importance of actin hydrophobic loop 262-274 dynamics to actin polymerization and filament stability has been shown recently with the use of the yeast mutant actin L180C/L269C/C374A, in which the hydrophobic loop could be locked in a "parked" conformation by a disulfide bond between C180 and C269. Such a cross-linked globular actin monomer does not form filaments, suggesting nucleation and/or elongation...

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Identifiers

PMID: 18037437
DOI: 10.1016/j.jmb.2007.10.076
PMCID: PMC4022318

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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