2xdw | pdb_00002xdw
From Proteopedia
Inhibition of Prolyl Oligopeptidase with a Synthetic Unnatural Dipeptide
| ||||||||||||
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA new inhibitor, containing a linked proline-piperidine structure, for the enzyme prolyl oligopeptidase (POP) has been synthesised and demonstrated to bind covalently with the enzyme at the active site. This provides evidence that covalent inhibitors of POP do not have to be limited to structures containing five-membered N-containing heterocyclic rings. Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.,Racys DT, Rea D, Fulop V, Wills M Bioorg Med Chem. 2010 Jul 1;18(13):4775-82. Epub 2010 May 31. PMID:20627594[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||||||
This page was last modified 14:15, 17 December 2014.