Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 7 July 1995:
Vol. 269. no. 5220, pp. 66 - 69
DOI: 10.1126/science.7604279
Prev | Table of Contents | Next

Articles

Science, Vol 269, Issue 5220, 66-69
Copyright © 1995 by American Association for the Advancement of Science

articles

Interaction of a peptidomimetic aminimide inhibitor with elastase

E Peisach, D Casebier, SL Gallion, P Furth, GA Petsko, JC Hogan Jr, and D Ringe

Program in Biophysics, Brandeis University, Waltham, MA 02254, USA.

The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques.
R. Brenke, D. Kozakov, G.-Y. Chuang, D. Beglov, D. Hall, M. R. Landon, C. Mattos, and S. Vajda (2009)
Bioinformatics 25, 621-627
   Abstract »    Full Text »    PDF »
Novel Mechanism of Inhibition of Elastase by beta -Lactams Is Defined by Two Inhibitor Crystal Complexes.
P. Taylor, V. Anderson, J. Dowden, S. L. Flitsch, N. J. Turner, K. Loughran, and M. D. Walkinshaw (1999)
J. Biol. Chem. 274, 24901-24905
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)