1J0X

Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)

1J0X の概要

• エントリーDOI: 10.2210/pdb1j0x/pdb
• 分子名称: glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, dehydrogenase, rossmann fold, mammalian gapdh, apoptosis, negative cooperativity
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm, cytosol : P46406
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 144349.91

構造登録者

Cowan-Jacob, S.W.,Kaufmann, M.,Anselmo, A.N.,Stark, W.,Grutter, M.G. (登録日: 2002-11-25, 公開日: 2003-12-09, 最終更新日: 2023-10-25)

主引用文献

Cowan-Jacob, S.W.,Kaufmann, M.,Anselmo, A.N.,Stark, W.,Grutter, M.G.
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.
Acta Crystallogr.,Sect.D, 59:2218-2227, 2003

PubMed Abstract: 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.

PubMed: 14646080
DOI: 10.1107/S0907444903020493

実験手法

X-RAY DIFFRACTION (2.4 Å)