Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
Article Abstract:
E2, the major protein regulator of the papillomaviruses' genetic transcription, attaches to its specific DNA target using a hitherto unknown dimeric antiparallel beta-barrel. The interaction of successive large grooves with two symmetrically arranged alpha-helices twists the DNA over the barrel. The E2-DNA interface consists of a complex of interactions in which the identifying base pairs of the target link to more than one amino-acid side chain and the selective amino acids react with more than one base pair.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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A new component of the transcription factor DRTF1/E2F
Article Abstract:
DRTF1/E2F, a transcription factor that controls the cell cycle's reactions with regulators of cellular growth such as retinoblastoma tumor-suppressor gene product, contains a complementary DNA that encodes DRTF1-polypeptide-1 (DP-1), an important sequence-specific binding protein. Further analysis indicated the presence of an additional binding protein since the DNA-binding domain of DP-1 includes a region similar to what is found in E2F-1 protein.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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