The crystal structure of the DNA-binding domain of vIRF-1 from the oncogenic KSHV reveals a conserved fold for DNA binding and reinforces its role as a transcription factor

• Published in: Nucleic acids research Vol. 41; no. 7; pp. 4295 - 4306
• Main Authors: Hew, Kelly, Dahlroth, Sue-Li, Venkatachalam, Rajakannan, Nasertorabi, Fariborz, Lim, Bee Ting, Cornvik, Tobias, Nordlund, Pär
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.04.2013
• Subjects: Cell- och molekylärbiologi; Crystallography, X-Ray; DNA - chemistry; DNA - metabolism; Interferon Regulatory Factors - chemistry; Interferon Regulatory Factors - metabolism; Medicin och hälsovetenskap; Medicinska och farmaceutiska grundvetenskaper; Models, Molecular; Protein Folding; Protein Structure, Tertiary; Structural Biology; Viral Proteins - chemistry; Viral Proteins - metabolism

Kaposi's sarcoma-associated herpesvirus encodes four viral homologues to cellular interferon regulatory factors (IRFs), where the most studied is vIRF-1. Even though vIRF-1 shows sequence homology to the N-terminal DNA-binding domain (DBD) of human IRFs, a specific role for this domain in vIRF-...