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Article

Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.

The Journal of biological chemistry - 28 Sept 2012

Padilla-Meier G Pauline, Gilcrease Eddie B, Weigele Peter R, Cortines Juliana R, Siegel Molly, Leavitt Justin C, Teschke Carolyn M, Casjens Sherwood R

Abstract excerpt

Many viruses encode scaffolding and coat proteins that co-assemble to form procapsids, which are transient precursor structures leading to progeny virions. In bacteriophage P22, the association of scaffolding and coat proteins is mediated mainly by ionic interactions. The coat protein-binding domain of scaffolding protein is a helix turn helix structure near the C terminus with a high number of charged surface...

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Identifiers

PMID: 22879595
DOI: 10.1074/jbc.M112.393132
PMCID: PMC3460473

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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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