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| | ==High resolution structure of TbPTR1 with trimetrexate== | | ==High resolution structure of TbPTR1 with trimetrexate== |
| - | <StructureSection load='2x9v' size='340' side='right' caption='[[2x9v]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='2x9v' size='340' side='right'caption='[[2x9v]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x9v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trybb Trybb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X9V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x9v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TMQ:TRIMETREXATE'>TMQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x9n|2x9n]], [[2vz0|2vz0]], [[2c7v|2c7v]], [[2wd7|2wd7]], [[2wd8|2wd8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TMQ:TRIMETREXATE'>TMQ</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pteridine_reductase Pteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.33 1.5.1.33] </span></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=2x9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9v OCA], [https://pdbe.org/2x9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9v RCSB], [https://www.ebi.ac.uk/pdbsum/2x9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9v ProSAT]</span></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=2x9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9v OCA], [http://pdbe.org/2x9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x9v RCSB], [http://www.ebi.ac.uk/pdbsum/2x9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O76290_TRYBB O76290_TRYBB] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pteridine reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Trybb]] | + | [[Category: Trypanosoma brucei brucei]] |
| - | [[Category: Barrack, K L]] | + | [[Category: Barrack KL]] |
| - | [[Category: Dawson, A]] | + | [[Category: Dawson A]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Tulloch, L B]] | + | [[Category: Tulloch LB]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short chain dehydrogenase]]
| + | |
| Structural highlights
Function
O76290_TRYBB
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
Pteridine reductase (PTR1) is a potential target for drug development against parasitic Trypanosoma and Leishmania species. These protozoa cause serious diseases for which current therapies are inadequate. High-resolution structures have been determined, using data between 1.6 and 1.1 A resolution, of T. brucei PTR1 in complex with pemetrexed, trimetrexate, cyromazine and a 2,4-diaminopyrimidine derivative. The structures provide insight into the interactions formed by new molecular entities in the enzyme active site with ligands that represent lead compounds for structure-based inhibitor development and to support early-stage drug discovery.
High-resolution structures of Trypanosoma brucei pteridine reductase ligand complexes inform on the placement of new molecular entities in the active site of a potential drug target.,Dawson A, Tulloch LB, Barrack KL, Hunter WN Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1334-40. Epub 2010, Nov 16. PMID:21123874[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dawson A, Tulloch LB, Barrack KL, Hunter WN. High-resolution structures of Trypanosoma brucei pteridine reductase ligand complexes inform on the placement of new molecular entities in the active site of a potential drug target. Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1334-40. Epub 2010, Nov 16. PMID:21123874 doi:10.1107/S0907444910040886
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