Display Settings:

Format

Send to:

Choose Destination
    EMBO Rep. 2011 Apr;12(4):334-41. Epub 2011 Mar 11.

    Structure and function of a HECT domain ubiquitin-binding site.

    Source

    Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712, USA.

    Abstract

    The Rsp5 ubiquitin ligase contains a non-covalent binding site for ubiquitin within the amino-terminal lobe (N-lobe) of the HECT domain, and the X-ray crystal structure of the HECT-ubiquitin complex has been determined. Hydrophobic patch residues of ubiquitin (L8, I44, V70) were crucial for interaction with Rsp5, and amino-acid alterations at the Rsp5-binding interface resulted in defects in polyubiquitination. Our results support a model in which the N-lobe-binding site acts to localize and orient the distal end of the ubiquitin chain to promote conjugation of the next ubiquitin molecule.

    PMID:
    21399621
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3077248
    Free PMC Article

      Supplemental Content

      Icon for Nature Publishing Group Icon for PubMed Central

      Save items

      loading

      Structures reported by this article

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk