1sej
From Proteopedia
(New page: 200px<br /><applet load="1sej" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sej, resolution 2.87Å" /> '''Crystal Structure of...) |
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| - | [[Image:1sej.gif|left|200px]]<br /><applet load="1sej" size=" | + | [[Image:1sej.gif|left|200px]]<br /><applet load="1sej" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sej, resolution 2.87Å" /> | caption="1sej, resolution 2.87Å" /> | ||
'''Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP'''<br /> | '''Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cryptosporidium hominis is a protozoan parasite that causes acute | + | 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== | ==About this Structure== | ||
| - | 1SEJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis] with UMP, F89 and NDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SEJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis] with <scene name='pdbligand=UMP:'>UMP</scene>, <scene name='pdbligand=F89:'>F89</scene> and <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEJ OCA]. |
==Reference== | ==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 | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511011 16511011] |
[[Category: Cryptosporidium hominis]] | [[Category: Cryptosporidium hominis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, A | + | [[Category: Anderson, A C.]] |
[[Category: F89]] | [[Category: F89]] | ||
[[Category: NDP]] | [[Category: NDP]] | ||
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[[Category: bifunctional enzyme]] | [[Category: bifunctional enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:42 2008'' |
Revision as of 13:00, 21 February 2008
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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 with , and as ligands. 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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