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Article

Crystal structure of the gamma-2 herpesvirus LANA DNA binding domain identifies charged surface residues which impact viral latency.

PLoS pathogens - 1 Jan 2013

Correia Bruno, Cerqueira Sofia A, Beauchemin Chantal, Pires de Miranda Marta, Li Shijun, Ponnusamy Rajesh, Rodrigues Lénia, Schneider Thomas R, Carrondo Maria A, Kaye Kenneth M, Simas J Pedro, McVey Colin E

Abstract excerpt

Latency-associated nuclear antigen (LANA) mediates γ2-herpesvirus genome persistence and regulates transcription. We describe the crystal structure of the murine gammaherpesvirus-68 LANA C-terminal domain at 2.2 Å resolution. The structure reveals an alpha-beta fold that assembles as a dimer, reminiscent of Epstein-Barr virus EBNA1. A predicted DNA binding surface is present and opposite this interface is a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 24146618
DOI: 10.1371/journal.ppat.1003673
PMCID: PMC3798461

Genes

BRD4

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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