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

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

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, remini...

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Autores principales: Bruno Correia, Sofia A Cerqueira, Chantal Beauchemin, Marta Pires de Miranda, Shijun Li, Rajesh Ponnusamy, Lénia Rodrigues, Thomas R Schneider, Maria A Carrondo, Kenneth M Kaye, J Pedro Simas, Colin E McVey
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
Materias:
Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Acceso en línea:https://doaj.org/article/e9ab2330f422454c8330e6d4aa52cb19
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https://doaj.org/article/e9ab2330f422454c8330e6d4aa52cb19

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