Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DMA-binding domain bound to its DNA target
Copyright policy )Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DMA-binding domain bound to its DNA target
The dominant transcriptional regulator of the papillomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric antiparallel beta-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed alpha-helices. The specific interface is an 'interwoven' network of interactions where the identifying base pairs of the target contact more than one amino-acid side chain and the discriminating amino acids interact with more than one base pair.
- Brigham and Women's Faulkner Hospital United States
- Yale University United States
- Howard Hughes Medical Institute United States
- University of Chicago United States
Models, Molecular, Protein Folding, Binding Sites, Base Sequence, Molecular Structure, Macromolecular Substances, Molecular Sequence Data, Hydrogen Bonding, DNA, DNA-Binding Proteins, Viral Proteins, Nucleic Acid Conformation, Amino Acid Sequence, Crystallization, Bovine papillomavirus 1
Models, Molecular, Protein Folding, Binding Sites, Base Sequence, Molecular Structure, Macromolecular Substances, Molecular Sequence Data, Hydrogen Bonding, DNA, DNA-Binding Proteins, Viral Proteins, Nucleic Acid Conformation, Amino Acid Sequence, Crystallization, Bovine papillomavirus 1
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