2xdw

Inhibition of Prolyl Oligopeptidase with a Synthetic Unnatural Dipeptide

spinqualitylabelsall models 2xdw, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xdw is a 2 chain structure with sequence from Sus scrofa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: GOL, PHQ, TAM, YCP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PPCE_PIG 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 A 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Prolyl Endopeptidase

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