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Article

A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.

The Journal of biological chemistry - 5 Apr 2013

Barua Bipasha, Fagnant Patricia M, Winkelmann Donald A, Trybus Kathleen M, Hitchcock-DeGregori Sarah E

Abstract excerpt

Actin filament cytoskeletal and muscle functions are regulated by actin binding proteins using a variety of mechanisms. A universal actin filament regulator is the protein tropomyosin, which binds end-to-end along the length of the filament. The actin-tropomyosin filament structure is unknown, but there are atomic models in different regulatory states based on electron microscopy reconstructions, computational...

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Identifiers

PMID: 23420843
DOI: 10.1074/jbc.M113.451161
PMCID: PMC3617264

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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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A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.PMID 23420843Read ↗

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