1j0x
From Proteopedia
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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 NAD 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 Tue Nov 20 17:50:46 2007
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
