Interactions of the helix-turn-helix binding domain. Current opinion in structural biology 1991, 1:80-88

Journal Article (Journal Article)

Recent studies of members of the helix-turn-helix class of DNA-binding proteins have indicated the importance of non-specific protein-phosphate 'positioning contacts' and revealed several novel features of protein-DNA recognition and binding. These novel features include: the dramatic change in the quaternary structure of Cro (the Cro protein of bacteriophage λ) on binding specifically to DNA; the striking bending of DNA by the catabolite gene activator protein; the dependence of the DNA-binding specificity of homeodomains on the nature of a single residue of the helix-turn-helix motif; and the specific recognition of minor-groove base pairs by the product of the engrailed gene of Drosophila. © 1991.

Full Text

Duke Authors

Cited Authors

  • Brennan, RG

Published Date

  • January 1, 1991

Published In

Volume / Issue

  • 1 / 1

Start / End Page

  • 80 - 88

International Standard Serial Number (ISSN)

  • 0959-440X

Digital Object Identifier (DOI)

  • 10.1016/0959-440X(91)90015-L

Citation Source

  • Scopus