1j0x
From Proteopedia
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|PDB= 1j0x |SIZE=350|CAPTION= <scene name='initialview01'>1j0x</scene>, resolution 2.4Å | |PDB= 1j0x |SIZE=350|CAPTION= <scene name='initialview01'>1j0x</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | + | |LIGAND= <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> |
- | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0x OCA], [http://www.ebi.ac.uk/pdbsum/1j0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j0x RCSB]</span> | ||
}} | }} | ||
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[[Category: Kaufmann, M.]] | [[Category: Kaufmann, M.]] | ||
[[Category: Stark, W.]] | [[Category: Stark, W.]] | ||
- | [[Category: NAD]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:22 2008'' |
Revision as of 18:27, 30 March 2008
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, resolution 2.4Å | |||||||
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Ligands: | , , | ||||||
Activity: | Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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 Sun Mar 30 21:27:22 2008