Structural highlights
Function
[CELA1_PIG] Acts upon elastin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Interaction of a peptidomimetic aminimide inhibitor with elastase.,Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D Science. 1995 Jul 7;269(5220):66-9. PMID:7604279[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D. Interaction of a peptidomimetic aminimide inhibitor with elastase. Science. 1995 Jul 7;269(5220):66-9. PMID:7604279
