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== | ==Phosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparum== | ||
[[http://www.uniprot.org/uniprot/AMP1_PLAFQ AMP1_PLAFQ | <StructureSection load='4k5l' size='340' side='right'caption='[[4k5l]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4k5l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_FcB1/Columbia Plasmodium falciparum FcB1/Columbia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K5L FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=19N:[(1R)-1-AMINO-5-CARBAMIMIDAMIDOPENTYL]PHOSPHONIC+ACID'>19N</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k5l OCA], [https://pdbe.org/4k5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k5l RCSB], [https://www.ebi.ac.uk/pdbsum/4k5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k5l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMP1_PLAFQ 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.<ref>PMID:12166515</ref> <ref>PMID:19196988</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23713488</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[ | <div class="pdbe-citations 4k5l" style="background-color:#fffaf0;"></div> | ||
[[Category: | ==See Also== | ||
[[Category: | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium falciparum FcB1/Columbia]] | |||
[[Category: McGowan S]] | |||
Latest revision as of 18:54, 20 September 2023
Phosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparumPhosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparum
Structural highlights
FunctionAMP1_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.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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