Interaction of a Peptidomimetic Aminimide Inhibitor with Elastase

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 s...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1995-07, Vol.269 (5220), p.66-69
Main Authors: Peisach, Ezra, Casebier, David, Gallion, Steven L., Furth, Paul, Petsko, Gregory A., Hogan, Joseph C., Ringe, Dagmar
Format: Article
Language:English
Subjects:
Active sites
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Anilides
Anilides - chemistry
Anilides - metabolism
Atoms
Binding Sites
Biological and medical sciences
Crystallography, X-Ray
Crystals
Dipeptides - chemistry
Dipeptides - metabolism
Drugs
Elastases
Electron density
Enzymes
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrazines - chemistry
Hydrazines - metabolism
Hydrogen Bonding
Hydrogen bonds
Hydrolases
Inhalants
Inhibition
Innovations
Ions
Medical research
Molecular Sequence Data
Molecules
Nitrogen
Organic Chemistry
Pancreas
Pancreatic Elastase - antagonists & inhibitors
Pancreatic Elastase - chemistry
Pancreatic Elastase - metabolism
Peptides
Peptidomimetics
Pharmaceutical research
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7604279