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Article

The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.

The Journal of biological chemistry - 11 Oct 2013

Krumm Stefanie A, Takeda Makoto, Plemper Richard K

Abstract excerpt

Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surface. A molecular recognition element (MoRE) domain mediates binding of the viral phosphoprotein (P). This P N-tail...

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Identifiers

PMID: 24003217
DOI: 10.1074/jbc.M113.503862
PMCID: PMC3795292

Provenance

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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