The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1.

Proteins 2020 Jan 1;88(1):106-112. Epub 2019 Aug 1.

Laboratório de Cristalografia, Physics Department, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil.

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 P3 21. 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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http://dx.doi.org/10.1002/prot.25773DOI Listing
January 2020

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References

(Supplied by CrossRef)
Genetic analysis of the activation domain of bovine papillomavirus protein E2: its role in transcription and replication
Ferguson MK et al.
J Virol 1996
Sequences flanking the core DNA‐binding domain of bovine papillomavirus type 1 E2 contribute to DNA‐binding function
Pepinsky RB et al.
J Virol 1997

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