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Article

Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif.

The Journal of biological chemistry - 3 Dec 2004

Corcoran Jennifer A, Syvitski Raymond, Top Deniz, Epand Richard M, Epand Raquel F, Jakeman David, Duncan Roy

Abstract excerpt

Members of the fusion-associated small transmembrane (FAST) protein family are a distinct class of membrane fusion proteins encoded by nonenveloped fusogenic reoviruses. The 125-residue p14 FAST protein of reptilian reovirus has an approximately 38-residue myristoylated N-terminal ectodomain containing a moderately apolar N-proximal region, termed the hydrophobic patch. Mutagenic analysis indicated...

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Identifiers

PMID: 15448165
DOI: 10.1074/jbc.M406990200

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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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