X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity
- 10 November 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 303 (5) , 745-760
- https://doi.org/10.1006/jmbi.2000.4181
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiaeJournal of Molecular Biology, 1997
- A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasiticaProtein Science, 1994
- Crystallization and Preliminary Crystallographic Characterization of Aspartic Proteinase-A from Baker's Yeast and Its Complexes with InhibitorsJournal of Molecular Biology, 1993
- Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.Proceedings of the National Academy of Sciences, 1993
- Design and synthesis of potent, selective, and orally active fluorine-containing renin inhibitorsJournal of Medicinal Chemistry, 1992
- The Structure and Function of the Aspartic ProteinasesAnnual Review of Biophysics, 1990
- Substrate specificity of proteinase yscA from Saccharomyces cerevisiaeCarlsberg Research Communications, 1989
- PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors.Molecular and Cellular Biology, 1986
- Yeast proteinase in beerCarlsberg Research Communications, 1983
- A new least-squares refinement technique based on the fast Fourier transform algorithmActa Crystallographica Section A, 1978