4gr1: Difference between revisions
New page: left|200px<br /> <applet load="4gr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="4gr1, resolution 2.4Å" /> '''THE BINDING OF THE R... |
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[[Image:4gr1.gif|left|200px]]<br /> | [[Image:4gr1.gif|left|200px]]<br /><applet load="4gr1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="4gr1, resolution 2.4Å" /> | caption="4gr1, resolution 2.4Å" /> | ||
'''THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE'''<br /> | '''THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
The retro-analogue of glutathione disulfide was bound to the GSSG binding | The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained. | ||
==Disease== | ==Disease== | ||
Known | Known diseases associated with this structure: Hemolytic anemia due to glutathione reductase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138300 138300]], Mental retardation, autosomal recessive, 6 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138244 138244]] | ||
==About this Structure== | ==About this Structure== | ||
4GR1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4, FAD and RGS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] Full crystallographic information is available from [http:// | 4GR1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=RGS:'>RGS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GR1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Janes, W.]] | [[Category: Janes, W.]] | ||
[[Category: Schulz, G | [[Category: Schulz, G E.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
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[[Category: oxidoreductase (flavoenzyme)]] | [[Category: oxidoreductase (flavoenzyme)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:27 2008'' | ||
Revision as of 20:13, 21 February 2008
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THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE
OverviewOverview
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
DiseaseDisease
Known diseases associated with this structure: Hemolytic anemia due to glutathione reductase deficiency OMIM:[138300], Mental retardation, autosomal recessive, 6 OMIM:[138244]
About this StructureAbout this Structure
4GR1 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Glutathione-disulfide reductase, with EC number 1.8.1.7 Full crystallographic information is available from OCA.
ReferenceReference
The binding of the retro-analogue of glutathione disulfide to glutathione reductase., Janes W, Schulz GE, J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009
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