1j0x
From Proteopedia
(New page: 200px<br /><applet load="1j0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j0x, resolution 2.4Å" /> '''Crystal structure of ...) |
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| - | [[Image:1j0x.gif|left|200px]]<br /><applet load="1j0x" size=" | + | [[Image:1j0x.gif|left|200px]]<br /><applet load="1j0x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j0x, resolution 2.4Å" /> | caption="1j0x, resolution 2.4Å" /> | ||
'''Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)'''<br /> | '''Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the tetrameric form of | + | The crystal structure of the tetrameric form of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isolated from rabbit muscle was solved at 2.4 A resolution after careful dynamic light-scattering experiments to find a suitable buffer for crystallization trials. The refined model has a crystallographic R factor of 20.3%. Here, the first detailed model of a mammalian GAPDH is presented. The cofactor NAD(+) (nicotinamide adenine dinucleotide) is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD(+) binding to this enzyme. The structure of rabbit-muscle GAPDH is of interest because it shares 91% sequence identity with the human enzyme; human GAPDH is a potential target for the development of anti-apoptotic drugs. In addition, differences in the cofactor-binding pocket compared with the homology-model structure of GAPDH from the malaria parasite Plasmodium falciparum could be exploited in order to develop novel selective and potential antimalaria drugs. |
==About this Structure== | ==About this Structure== | ||
| - | 1J0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http:// | + | 1J0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J0X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anselmo, A | + | [[Category: Anselmo, A N.]] |
| - | [[Category: Cowan-Jacob, S | + | [[Category: Cowan-Jacob, S W.]] |
| - | [[Category: Grutter, M | + | [[Category: Grutter, M G.]] |
[[Category: Kaufmann, M.]] | [[Category: Kaufmann, M.]] | ||
[[Category: Stark, W.]] | [[Category: Stark, W.]] | ||
| Line 27: | Line 27: | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:46 2008'' |
Revision as of 11:17, 21 February 2008
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Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
Overview
The crystal structure of the tetrameric form of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isolated from rabbit muscle was solved at 2.4 A resolution after careful dynamic light-scattering experiments to find a suitable buffer for crystallization trials. The refined model has a crystallographic R factor of 20.3%. Here, the first detailed model of a mammalian GAPDH is presented. The cofactor NAD(+) (nicotinamide adenine dinucleotide) is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD(+) binding to this enzyme. The structure of rabbit-muscle GAPDH is of interest because it shares 91% sequence identity with the human enzyme; human GAPDH is a potential target for the development of anti-apoptotic drugs. In addition, differences in the cofactor-binding pocket compared with the homology-model structure of GAPDH from the malaria parasite Plasmodium falciparum could be exploited in order to develop novel selective and potential antimalaria drugs.
About this Structure
1J0X is a Single protein structure of sequence from Oryctolagus cuniculus with as ligand. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.
Reference
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase., Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2218-27. Epub 2003, Nov 27. PMID:14646080
Page seeded by OCA on Thu Feb 21 13:17:46 2008
Categories: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) | Oryctolagus cuniculus | Single protein | Anselmo, A N. | Cowan-Jacob, S W. | Grutter, M G. | Kaufmann, M. | Stark, W. | NAD | Apoptosis | Dehydrogenase | Mammalian gapdh | Negative cooperativity | Oxidoreductase | Rossmann fold
