Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5

Kirk L. Clark, Elaine D. Halay, Eseng Lai, Stephen K. Burley

Research output: Contribution to journalArticlepeer-review

1035 Scopus citations

Abstract

The three-dimensional structure of an HNF-3/fork head DNA-recognition motif complexed with DNA has been determined by X-ray crystallography at 2.5 Å resolution. This α/β protein binds B-DNA as a monomer, through interactions with the DNA backbone and through both direct and water-mediated major and minor groove base contacts, inducing a 13°bend. The transcription factor fold is very similar to the structure of histone H5. In its amino-terminal half, three α-helices adopt a compact structure that presents the third helix to the major groove. The remainder of the protein includes a twisted, antiparallel β-structure and random coil that interacts with the minor groove.

Original languageEnglish (US)
Pages (from-to)412-420
Number of pages9
JournalNature
Volume364
Issue number6436
DOIs
StatePublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • General

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