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

• Main Authors: Hew, Kelly, Dahlroth, Sue-Li, Venkatachalam, Rajakannan, Nasertorabi, Fariborz, Lim, Bee Ting, Cornvik, Tobias Carl, Nordlund, Pär
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2013
• Subjects: DRNTU::Science::Biological sciences::Genetics
• Online Access: https://hdl.handle.net/10356/96960; http://hdl.handle.net/10220/9985
• Institution: Nanyang Technological University

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-1’s f...