1sej

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[[Image:1sej.gif|left|200px]]
[[Image:1sej.gif|left|200px]]
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{{Structure
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|PDB= 1sej |SIZE=350|CAPTION= <scene name='initialview01'>1sej</scene>, resolution 2.87&Aring;
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The line below this paragraph, containing "STRUCTURE_1sej", creates the "Structure Box" on the page.
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|SITE=
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|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&#39;-DEOXYURIDINE+5&#39;-MONOPHOSPHATE'>UMP</scene>
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{{STRUCTURE_1sej| PDB=1sej | SCENE= }}
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|RELATEDENTRY=[[1qzf|1qzf]]
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|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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'''Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP'''
'''Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Anderson, A C.]]
[[Category: Anderson, A C.]]
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[[Category: bifunctional enzyme]]
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[[Category: Bifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:36:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:59 2008''
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Revision as of 05:36, 3 May 2008

Image:1sej.gif

Template:STRUCTURE 1sej

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 Page seeded by OCA on Sat May 3 08:36:38 2008

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