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

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 p...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2020-01, Vol.88 (1), p.106-112
Main Authors: Leroy, Ludmila, Barbosa, João Alexandre Ribeiro Gonçalves, Prat‐Gay, Gonzalo, Polikarpov, Igor, Pinheiro, Carlos Basílio
Format: Article
Language:English
Subjects:
Binding
bovine papillomavirus
Crystal structure
Deoxyribonucleic acid
Dimers
DNA
E2 DNA‐binding domain
Human papillomavirus
LI loop
protein structure
Proteins
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Summary: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.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.25773