Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Bovine papillomavirus 1 / genetics*
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Crystallization
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DNA / chemistry
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DNA / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism
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Hydrogen Bonding
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Macromolecular Substances
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Models, Molecular
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Molecular Sequence Data
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Molecular Structure
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Nucleic Acid Conformation
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Protein Folding
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Viral Proteins / chemistry*
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Viral Proteins / metabolism
Substances
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DNA-Binding Proteins
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E2 protein, Bovine papillomavirus
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Macromolecular Substances
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Viral Proteins
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DNA