Structural highlights
Publication Abstract from PubMed
The latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.
Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.,Hellert J, Krausze J, Schulz TF, Luhrs T Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1570-4. doi:, 10.1107/S2053230X14019906. Epub 2014 Oct 25. PMID:25372834[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hellert J, Krausze J, Schulz TF, Luhrs T. Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1570-4. doi:, 10.1107/S2053230X14019906. Epub 2014 Oct 25. PMID:25372834 doi:http://dx.doi.org/10.1107/S2053230X14019906