Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 88, Issue 1, Pages 106-112Publisher
WILEY
DOI: 10.1002/prot.25773
Keywords
bovine papillomavirus; E2 DNA-binding domain; LI loop; protein structure
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Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico [309086/2016-7, 477789/2008-0]
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Bovine papillomavirus proteins were extensively studied as a prototype for the human papillomavirus. Here, the crystal structure of the extended E2 DNA-binding domain of the dominant transcription regulator from the bovine papillomavirus strain 1 is described in the space group P3121. We found two protein functional dimers packed in the asymmetric unit. This new protein arrangement inside the crystal led to the reduction of the mobility of a previously unobserved loop directly involved in the protein-DNA interaction, which was then modeled for the first time.
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