AI Article Synopsis
- Researchers studied bovine papillomavirus proteins to gain insights into human papillomavirus.
- The crystal structure of the E2 DNA-binding domain from bovine papillomavirus was analyzed, revealing a specific arrangement of protein dimers.
- This new configuration reduced the movement of a loop essential for protein-DNA interaction, allowing for its modeling for the first time.
Article Abstract
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.25773 | DOI Listing |
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