Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Nature. 1987 Jun 18-24;327(6123):591-7.

The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.

Abstract

Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits.

PMID:
3600756
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Write to the Help Desk