Structural highlights
Function
[PPCE_HUMAN] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
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
We report the synthesis and in vitro activity of a series of novel pyrrolidinyl pyridones and pyrazinones as potent inhibitors of prolyl oligopeptidase (POP). Within this series, compound 39 was co-crystallized within the catalytic site of a human chimeric POP protein which provided a more detailed understanding of how these inhibitors interacted with the key residues within the catalytic pocket.
Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP).,Haffner CD, Diaz CJ, Miller AB, Reid RA, Madauss KP, Hassell A, Hanlon MH, Porter DJ, Becherer JD, Carter LH Bioorg Med Chem Lett. 2008 Aug 1;18(15):4360-3. Epub 2008 Jun 24. PMID:18606544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haffner CD, Diaz CJ, Miller AB, Reid RA, Madauss KP, Hassell A, Hanlon MH, Porter DJ, Becherer JD, Carter LH. Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP). Bioorg Med Chem Lett. 2008 Aug 1;18(15):4360-3. Epub 2008 Jun 24. PMID:18606544 doi:10.1016/j.bmcl.2008.06.067
