X-RAY CRYSTAL ANALYSIS OF THE HUMAN PAPILLOMA VIRUS TYPE-11 E2-BS. James Finley, Ming Luo, University of Alabama-Birmingham, Center for Macromolecular Crystallography, Birmingham, AL USA

The human papilloma viruses, the viruses responsible for common warts, have also been implicated in cancers such as cervical carcinoma. E2, a viral transcription factor, is responsible for regulating both replication of the viral genome and transcription of viral genes including the oncogenic E6 protein. This regulation is accomplished by E2 associating with a specific DNA binding site in the viral genome called the E2 binding site (E2-BS). The sequence E2 bindings is ACCN₆GGT where N is any nucleotide. By studying the interaction of the E2 protein with the E2-BS, a deeper understanding of how the virus regulates transcription and replication may be achieved. To Characterize the Human Papilloma Virus Type-ll E2 protein's structure and function by X-ray crystallography, three crystallization trials are underway. These include the 207 amino acid N-terminal domain of the E2 protein, the 80 amino acid C-terminal domain of the E2 protein complexed with the E2-BS DNA, and the E2-BS DNA alone. Presently, the DNA sequence dGACCGCGGTC which contains the conserved ACC portion of the E2-BS has been crystallized and x-ray diffraction data has been collected. The crystals diffract to 1.5Å and appear to be primitive hexagonal.