My NCBISign In

Display Settings:

Format

Send to:

Choose Destination
    Structure. 2008 Nov 12;16(11):1616-25.

    Protein metamorphosis: the two-state behavior of Mad2.

    Luo X, Yu H.

    Source

    Department of Pharmacology, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390, USA. xuelian.luo@utsouthwestern.edu

    Abstract

    A given protein generally has only one native tertiary fold, which is the conformation with the lowest Gibbs free energy. Mad2, a protein involved in the spindle checkpoint, however, has two natively folded states with similar Gibbs free energies. Through binding to its target Cdc20, Mad2 inhibits the multisubunit ubiquitin ligase, the anaphase-promoting complex or cyclosome (APC/C), and delays the onset of anaphase until all sister chromatids achieve bipolar attachment to the mitotic spindle. Without ligand binding or covalent modifications, Mad2 adopts two topologically and functionally distinct native folds in equilibrium under physiological conditions. The transition between the two Mad2 states is regulated by multiple mechanisms and is central to the activation and inactivation of the spindle checkpoint. This review summarizes recent structural and biochemical studies on the two-state behavior of Mad2 and discusses the generality and implications of structural malleability of proteins.

    PMID:
    19000814
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2644451
    Free PMC Article

    Images from this publication.See all images (8) Free text

    Figure 1
    Figure 3
    Figure 5
    Figure 7
    Figure 2
    Figure 4
    Figure 6
    Figure 8

    Publication Types, MeSH Terms, Substances, Grant Support

    Publication Types

    MeSH Terms

    Substances

    Grant Support

    LinkOut - more resources

    Full Text Sources

    Other Literature Sources

      Supplemental Content

      Icon for Elsevier Science Icon for PubMed Central

      Save items

      loading

      Related citations in PubMed

      See reviews... See all...

      Cited by 11 PubMed Central articles

      See all...

      Structures reported by this article

      Related information

      • Related Citations
        Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
      • References for this PMC Article
        Citation referenced in PubMed article. Only valid for PubMed citations that are also in PMC.
      • Taxonomy via GenBank
        Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
      • Protein
        Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.
      • Structure
        Three-dimensional structure records in the NCBI Structure database for data reported in the current articles.
      • Free in PMC
        Free full text articles in PMC
      • Cited in PMC
        Full-text articles in the PubMed Central Database that cite the current articles.

      Recent activity

      Clear Turn Off Turn On

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      You are here: NCBI > Literature > PubMed
      Write to the Help Desk