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

@inproceedings{Hew2013TheCS,
  title={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},
  author={Kelly Hew and Sue-Li Dahlroth and Rajakannan Venkatachalam and Fariborz Nasertorabi and Bee Ting Lim and Tobias Cornvik and Paer Nordlund},
  booktitle={Nucleic acids research},
  year={2013}
}
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 function has remained uncertain. To provide insights into the function of the vIRF-1 DBD, we have determined the crystal structure of it in complex with DNA and in its apo-form. Using a thermal… CONTINUE READING
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