Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell. 2003 Jan 24;112(2):142-4.

Ubiquitinating a phosphorylated Cdk inhibitor on the blades of the Cdc4 beta-propeller.

Author information

  • 1Programs in Chemical Biology and Cancer Biology and Department of Pathology, Stanford University School of Medicine, 300 Pasteur Drive, Stanford, CA 94305, USA.

Abstract

Substrate binding by the SCFCdc4 ubiquitin ligase is regulated by phosphorylation. In this issue of Cell, Orlicky et al. describe the crystal structure of the Cdc4 subunit bound to a high-affinity substrate phosphopeptide. This structure provides insights into the binding interaction and how a precise mechanism involving multiple regulatory phosphorylations may be mediated by a single binding site.

PMID:
12553901
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Write to the Help Desk