Guo, J. and Erskine, Peter T. and Coker, A.R. and Wood, S.P. and Cooper, Jonathan B. (2015) Structure of a Kunitz-type potato cathepsin D inhibitor. Journal of Structural Biology 192 (3), pp. 554-560. ISSN 1047-8477.
Abstract
Potato cathepsin D inhibitor (PDI) is a glycoprotein of 188 amino acids which can inhibit both the aspartic protease cathepsin D and the serine protease trypsin. Here we report the first X-ray structure of PDI at a resolution of 2.1 Å showing that PDI adopts a β-trefoil fold, which is typical of the Kunitz-family protease inhibitors, with the inhibitory loops protruding from the core. Possible reactive-site loops including one involving a unique disulphide and another involving a protruding 310 helix are identified and docking studies indicate the mode of action this unusual bi-functional inhibitor.
Metadata
| Item Type: | Article |
|---|---|
| Additional Information: | Corrigendum at http://dx.doi.org/10.1016/j.jsb.2016.01.001 |
| Keyword(s) / Subject(s): | Potato cathepsin D inhibitor, Kunitz-type protease inhibitor, Protein X-ray structure, Reactive-site loop, Docking |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Birkbeck Knowledge Lab |
| Depositing User: | Administrator |
| Date Deposited: | 03 Nov 2015 17:54 |
| Last Modified: | 02 Aug 2023 17:19 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/13331 |
Statistics
Additional statistics are available via IRStats2.
Archive Staff Only (login required)
