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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Auteurs principaux: | , , , , , , , , , , , |
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Format: | article |
Langue: | EN |
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Public Library of Science (PLoS)
2013
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Accès en ligne: | https://doaj.org/article/e9ab2330f422454c8330e6d4aa52cb19 |
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