6kp2: Difference between revisions

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-'''Unreleased structure'''
-The entry 6kp2 is ON HOLD
+==Quadruple mutant plasmodium falciparum dihydrofolate reductase complexed with B10042==
+<StructureSection load='6kp2' size='340' side='right'caption='[[6kp2]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6kp2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KP2 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DQ3:5-(3-chlorophenyl)-6-(3-phenoxypropyl)pyrimidine-2,4-diamine'>DQ3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kp2 OCA], [http://pdbe.org/6kp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kp2 RCSB], [http://www.ebi.ac.uk/pdbsum/6kp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kp2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/D9N170_PLAFA D9N170_PLAFA]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The series of des-Cl (unsubstituted) and m-Cl phenyl analogues of PYR with various flexible 6-substituents were synthesized and studied for the binding affinities with highly resistant quadruple mutant (QM) DHFR. The derivatives carrying 4 atoms linker with a terminal carboxyl substituted on the aromatic ring exhibited good inhibition to the QM enzyme and also showed effective antimalarial activities against resistant P. falciparum bearing the mutant enzymes with relatively low cytotoxicity to mammalian cells. The X-ray crystallographic analysis of the enzyme-inhibitor complexes suggested that the hydrophobic substituent at 6-position was accommodated well in the hydrophobic pocket and the optimal length of the flexible linker could effectively promote the binding of the terminal carboxyl group to the key amino acid residues, Arg59 and Arg122.
-Authors:
+-Hydrophobic aromatic substituent pyrimethamine analogues as potential antimalarials for pyrimethamine-resistant Plasmodium falciparum.,Saepua S, Sadorn K, Vanichtanankul J, Anukunwithaya T, Rattanajak R, Vitsupakorn D, Kamchonwongpaisan S, Yuthavong Y, Thongpanchang C Bioorg Med Chem. 2019 Dec 15;27(24):115158. doi: 10.1016/j.bmc.2019.115158. Epub , 2019 Oct 28. PMID:31685330<ref>PMID:31685330</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6kp2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Vanichtanankul, J]]
+[[Category: Vitsupakorn, D]]
+[[Category: Antibiotic]]
+[[Category: Antifolate]]
+[[Category: Antimalarial]]
+[[Category: Dihydrofolate reductase]]
+[[Category: Oxidoreductase]]
+[[Category: Plasmodium falciparum]]
+[[Category: Transferase]]