Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Trends Biochem Sci. 2007 Feb;32(2):63-70. Epub 2007 Jan 8.

Sticky fingers: zinc-fingers as protein-recognition motifs.

Author information

  • 1School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.

Abstract

Zinc-fingers (ZnFs) are extremely abundant in higher eukaryotes. Once considered to function exclusively as sequence-specific DNA-binding motifs, ZnFs are now known to have additional activities such as the recognition of RNA and other proteins. Here we discuss recent advances in our understanding of ZnFs as specific modules for protein recognition. Structural studies of ZnF complexes reveal considerable diversity in terms of protein partners, binding modes and affinities, and highlight the often underestimated versatility of ZnF structure and function. An appreciation of the structural features of ZnF-protein interactions will contribute to our ability to engineer and to use ZnFs with tailored protein-binding properties.

PMID:
17210253
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk