Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Adaptation of the behaviour of an aspartic proteinase inhibitor by relocation of a lysine residue by one helical turn

Winterburn, Tim J., Wyatt, David M., Phylip, Lowri H., Berry, Colin, Bur, Daniel and Kay, John 2006. Adaptation of the behaviour of an aspartic proteinase inhibitor by relocation of a lysine residue by one helical turn. Biological Chemistry 387 (8) , pp. 1139-1142. 10.1515/BC.2006.140

Full text not available from this repository.

Abstract

In addition to self-inhibition of aspartic proteinase zymogens by their intrinsic proparts, the activity of certain members of this enzyme family can be modulated through active-site occupation by extrinsic polypeptides such as the small IA3 protein from Saccharomyces cerevisiae. The unprecedented mechanism by which IA3 helicates to inhibit its sole target aspartic proteinase locates an i, i+4 pair of charged residues (Lys18+Asp22) on an otherwise-hydrophobic face of the amphipathic helix. The nature of these residues is not crucial for effective inhibition, but re-location of the lysine residue by one turn (+4 residues) in the helical IA3 positions its side chain in the mutant IA3-proteinase complex in an orientation essentially identical to that of the key lysine residue in zymogen proparts. The binding of the extrinsic mutant IA3 shows pH dependence reminiscent of that required for the release of intrinsic zymogen proparts so that activation can occur.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > Q Science (General)
Publisher: Walter de Gruyter
ISSN: 1431-6730
Last Modified: 17 May 2019 21:38
URI: http://orca.cf.ac.uk/id/eprint/62583

Citation Data

Cited 7 times in Google Scholar. View in Google Scholar

Cited 6 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item