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2c5m
From Proteopedia
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CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE
Overview
Cytidine triphosphate synthetase (CTPS) is a key enzyme in nucleic acid and phospholipid biosynthesis and its activity is increased in certain human cancers, making it a promising drug target. The crystal structure of the synthetase domain of human CTPS, which represents the first structure of a CTPS from an eukaryote, has been determined. The structure is homotetrameric and each active site is formed by three different subunits. Sulfate ions bound to the active sites indicate the positions of phosphate-binding sites for the substrates ATP and UTP and the feedback inhibitor CTP. Together with earlier structures of bacterial CTPS, the human CTPS structure provides an extended understanding of the structure-function relationship of CTPS-family members. The structure also serves as a basis for structure-based design of anti-proliferative inhibitors.
About this Structure
2C5M is a Single protein structure of sequence from Homo sapiens with as ligand. Active as CTP synthase, with EC number 6.3.4.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of the synthetase domain of human CTP synthetase, a target for anticancer therapy., Kursula P, Flodin S, Ehn M, Hammarstrom M, Schuler H, Nordlund P, Stenmark P, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):613-7. Epub 2006 Jun 10. PMID:16820675
Page seeded by OCA on Thu Feb 21 16:45:10 2008
Categories: CTP synthase | Homo sapiens | Single protein | Arrowsmith, C. | Berg, S Van Den. | Berglund, H. | Edwards, A. | Ehn, M. | Flodin, S. | Graslund, S. | Hallberg, B M. | Hammarstrom, M. | Kotenyova, T. | Kursula, P. | Nilsson-Ehle, P. | Nordlund, P. | Ogg, D. | Persson, C. | Sagemark, J. | Schiavone, L Holmberg. | Schuler, H. | Stenmark, P. | Sundstrom, M. | Thorsell, A G. | Weigelt, J. | SO4 | Amidotransferase | Ctp | Ctp synthase | Ctp synthetase | Ctps | Cytidine 5-prime triphosphate synthetase | Glutamine | Ligase | Phosphorylation | Pyrimidine biosynthesis | Utp
