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PMID: 1328886 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target.

Nature ·Vol. 359 ·No. 6395 ·1992-10-08 ·Pages 505-12

Hegde RS, Grossman SR, Laimins LA, Sigler PB

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.

MeSH Terms
Amino Acid Sequence Base Sequence Binding Sites Bovine papillomavirus 1/genetics Crystallization DNA/chemistry,metabolism DNA-Binding Proteins/chemistry,metabolism Hydrogen Bonding Macromolecular Substances Models, Molecular Molecular Sequence Data Molecular Structure Nucleic Acid Conformation Protein Folding Viral Proteins/chemistry,metabolism
Chemicals
DNA-Binding Proteins E2 protein, Bovine papillomavirus Macromolecular Substances Viral Proteins DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hegde R S
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
Grossman S R
Laimins L A
Sigler P B
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-10-08
Pages
505-12
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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