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 porcine pancreatic elastase (PPE) complexed with a potent peptidyl inhibitor, FR136706, was solved at 2.2A resolution. FR136706 fits snugly into the extended active site pocket. The benzene moiety of FR136706 induced dramatic movement of the side chain moiety of Arg217 and both moieties formed a pi-pi interaction, which has never been found previously in structures of PPE complexed with inhibitors. This novel interaction mode may lead to design of new types of inhibitors.
True interaction mode of porcine pancreatic elastase with FR136706, a potent peptidyl inhibitor.,Kinoshita T, Nakanishi I, Sato A, Tada T Bioorg Med Chem Lett. 2003 Jan 6;13(1):21-4. PMID:12467609[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kinoshita T, Nakanishi I, Sato A, Tada T. True interaction mode of porcine pancreatic elastase with FR136706, a potent peptidyl inhibitor. Bioorg Med Chem Lett. 2003 Jan 6;13(1):21-4. PMID:12467609
