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

Rashmi S. Hegde*, Steven R. Grossman, Laimonis A. Laimins, Paul B. Sigler

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

316 Scopus citations

Abstract

The dominant transcriptional regulator of the papiIlomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric ant i para I lei β-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed α-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.

Original languageEnglish (US)
Pages (from-to)505-512
Number of pages8
JournalNature
Volume359
Issue number6395
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • General

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