4pnc

E. COLI METHIONINE AMINOPEPTIDASE IN COMPLEX WITH INHIBITOR 7-METHOXY-2-METHYLEN-3,4-DIHYDRONAPHTHALEN-1(2H)-ONE

spinqualitylabelsall models 4pnc, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pnc is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 7NP, CO, NA Related: 3mat, 1xnz, 1yvm Activity: Methionyl aminopeptidase, with EC number 3.4.11.18 Resources: FirstGlance, OCA, RCSB, PDBsum Function [C3TPN7_ECOLX] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity).[HAMAP-Rule:MF_01974] Publication Abstract from PubMed We identified and characterized beta-aminoketones as prodrugs for irreversible MetAP inhibitors that are selective for the MetAP-1 subtype. beta-Aminoketones with certain structural features form alpha,beta-unsaturated ketones under physiological conditions, which bind covalently and selectively to cysteines in the S1 pocket of MetAP-1. The binding mode was confirmed by X-ray crystallography and assays with the MetAPs from Escherichia coli, Staphylococcus aureus and both human isoforms. The initially identified tetralone derivatives showed complete selectivity for E. coli MetAP versus human MetAP-1 and MetAP-2. Rational design of indanone analogs yielded compounds with selectivity for the human type-1 versus the human type-2 MetAP. Beta-aminoketones as prodrugs for selective irreversible inhibitors of type-1 methionine aminopeptidases.,Altmeyer M, Amtmann E, Heyl C, Marschner A, Scheidig AJ, Klein CD Bioorg Med Chem Lett. 2014 Sep 23. pii: S0960-894X(14)00990-1. doi:, 10.1016/j.bmcl.2014.09.047. PMID:25293447 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase

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