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Article

The B30.2(SPRY) domain of the retroviral restriction factor TRIM5alpha exhibits lineage-specific length and sequence variation in primates.

Journal of virology - 1 May 2005

Song Byeongwoon, Gold Bert, O'Huigin Colm, Javanbakht Hassan, Li Xing, Stremlau Matthew, Winkler Cheryl, Dean Michael, Sodroski Joseph

Abstract excerpt

Tripartite motif (TRIM) proteins are composed of RING, B-box 2, and coiled coil domains. Some TRIM proteins, such as TRIM5alpha, also possess a carboxy-terminal B30.2(SPRY) domain and localize to cytoplasmic bodies. TRIM5alpha has recently been shown to mediate innate intracellular resistance to retroviruses, an activity dependent on the integrity of the B30.2 domain, in particular primate species. An examination...

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Source

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Identifiers

PMID: 15857996
DOI: 10.1128/JVI.79.10.6111-6121.2005
PMCID: PMC1091705

Genes

TRIM5

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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The B30.2(SPRY) domain of the retroviral restriction factor TRIM5alpha exhibits lineage-specific length and sequence variation in primates.PMID 15857996Read ↗

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Identification of a Genomic Reservoir for New TRIM Genes in Primate GenomesSemantic proximity Read ↗

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