1sej
From Proteopedia
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|PDB= 1sej |SIZE=350|CAPTION= <scene name='initialview01'>1sej</scene>, resolution 2.87Å | |PDB= 1sej |SIZE=350|CAPTION= <scene name='initialview01'>1sej</scene>, resolution 2.87Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=F89:S)-2-(5(((1,2-DIHYDRO-3-METHYL-1-OXOBENZO(F)QUINAZOLIN-9-YL)METHYL)AMINO)1-OXO-2-ISOINDOLINYL)GLUTARIC+ACID'>F89</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2'-DEOXYURIDINE+5'-MONOPHOSPHATE'>UMP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qzf|1qzf]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sej OCA], [http://www.ebi.ac.uk/pdbsum/1sej PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sej RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anderson, A C.]] | [[Category: Anderson, A C.]] | ||
| - | [[Category: F89]] | ||
| - | [[Category: NDP]] | ||
| - | [[Category: UMP]] | ||
[[Category: bifunctional enzyme]] | [[Category: bifunctional enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:59 2008'' |
Revision as of 20:41, 30 March 2008
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| , resolution 2.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1qzf
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP
Overview
Cryptosporidium hominis is a protozoan parasite that causes acute gastrointestinal illness. There are no effective therapies for cryptosporidiosis, highlighting the need for new drug-lead discovery. An analysis of the protein-ligand interactions in two crystal structures of dihydrofolate reductase-thymidylate synthase (DHFR-TS) from C. hominis, determined at 2.8 and 2.87 A resolution, reveals that the interactions of residues Ile29, Thr58 and Cys113 in the active site of C. hominis DHFR provide a possible structural basis for the observed antifolate resistance. A comparison with the structure of human DHFR reveals active-site differences that may be exploited for the design of species-selective inhibitors.
About this Structure
1SEJ is a Single protein structure of sequence from Cryptosporidium hominis. Full crystallographic information is available from OCA.
Reference
Two crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein-ligand interactions including a structural basis for observed antifolate resistance., Anderson AC, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt, 3):258-62. Epub 2005 Feb 8. PMID:16511011
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