4HLX
The crystal structure of the DNA binding domain of vIRF-1 from the oncogenic KSHV
Summary for 4HLX
| Entry DOI | 10.2210/pdb4hlx/pdb |
| Related | 4HLY |
| Descriptor | K9 (2 entities in total) |
| Functional Keywords | helix-turn-helix, dna binding protein |
| Biological source | Human herpesvirus 8 (HHV-8) |
| Total number of polymer chains | 4 |
| Total formula weight | 61237.92 |
| Authors | Hew, K.,Venkatachalam, R. (deposition date: 2012-10-17, release date: 2013-03-13, Last modification date: 2024-11-13) |
| Primary citation | Hew, K.,Dahlroth, S.L.,Venkatachalam, R.,Nasertorabi, F.,Lim, B.T.,Cornvik, T.,Nordlund, P. 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. Nucleic Acids Res., 41:4295-4306, 2013 Cited by PubMed Abstract: 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 stability shift assay (TSSA), we show that the vIRF-1 DBD binds DNA, whereas full-length vIRF-1 does not, suggesting a cis-acting regulatory mechanism in similarity to human IRFs. The complex structure of vIRF-1 DBD reveals interactions with the DNA backbone and the positioning of two arginines for specific recognition in the major grove. A superimposition with human IRF-3 reveals a similar positioning of the two specificity-determining arginines, and additional TSSAs indicate binding of vIRF-1 to an IRF-3 operator consensus sequence. The results from this study, therefore, provide support that vIRF-1 has evolved to bind DNA and plays a role in DNA binding in the context of transcriptional regulation and might act on some of the many operator sequences controlled by human IRF-3. PubMed: 23435230DOI: 10.1093/nar/gkt082 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.379 Å) |
Structure validation
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