4k5n

Phosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparum

spinqualitylabelsall models 4k5n, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4k5n is a 1 chain structure with sequence from Plasmodium falciparum FcB1/Columbia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: 1OU, GOL, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMP1_PLAFQ Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC. Publication Abstract from PubMed The malaria parasite <i>Plasmodium falciparum</i> employs two metallo-aminopeptidases, P<i>f</i>A-M1 and P<I>f</i>A-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new anti-malarial drugs. Here we report the synthesis and structure-activity-relationships of a small library of phosphonic acid arginine mimetics that probe the S1 pocket of both enzymes, and map the necessary interactions that would be important for a dual inhibitor. Synthesis and Structure-Activity Relationships of Phosphonic Arginine Mimetics as Inhibitors of the M1 and M17 Aminopeptidases from <i>Plasmodium falciparum</i>,Kannan Sivaraman K, Paiardini A, Sienczyk M, Ruggeri C, Oellig CA, Dalton JP, Scammells PJ, Drag M, McGowan S J Med Chem. 2013 May 28. PMID:23713488 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase 3D structures

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