Skip NavigationSkip to Content
Return Return to Search Results

The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix

  1. Author:
    Li, M.
    Phylip, L. H.
    Lees, W. E.
    Winther, J. R.
    Dunn, B. M.
    Wlodaawer, A.
    Kay, J.
    Gustchina, A.

  2. Author Address

    Kay J NCI, FCRDC, Program Struct Biol, Macromol Crystallog Lab Frederick, MD 21702 USA NCI, FCRDC, Program Struct Biol, Macromol Crystallog Lab Frederick, MD 21702 USA NCI, FCRDC, SAIC Frederick, Intramural Res Support Program Frederick, MD 21702 USA Cardiff Univ, Sch Biosci Cardiff CF1 3US S Glam Wales Carlsberg Res Lab, Dept Yeast Genet DK-2500 Copenhagen Valby Denmark Univ Florida, Dept Biochem & Mol Biol Gainesville, FL 32610 USA
    1. Year: 2000
  2. Journal: Nature Structural Biology
    1. 7
    2. 2
    3. Pages: 113-117
  4. Type of Article: Article
  1. Abstract:

    Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA(3) from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 Angstrom, respectively, for complexes of proteinase A with full-length IA(3) and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions, Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. [References: 31]

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel