2VO1

CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE

「2C5M」から置き換えられました

2VO1 の概要

• エントリーDOI: 10.2210/pdb2vo1/pdb
• 関連するPDBエントリー: 2C5M
• 分子名称: CTP SYNTHASE 1, SULFATE ION (3 entities in total)
• 機能のキーワード: pyrimidine biosynthesis, glutamine amidotransferase, phosphorylation, amidotransferase, cytidine 5-prime triphosphate synthetase, ctp, utp, ctps, ligase, glutamine, ctp synthase, phosphoprotein, ctp synthetase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66521.60

構造登録者

Stenmark, P.,Kursula, P.,Arrowsmith, C.,Berglund, H.,Edwards, A.,Ehn, M.,Flodin, S.,Graslund, S.,Hammarstrom, M.,Hallberg, B.M.,Holmberg-Schiavone, L.,Kotenyoa, T.,Moche, M.,Nilsson-Ehle, P.,Ogg, D.,Persson, C.,Sagemark, J.,Schuler, H.,Sundstrom, M.,Thorsell, A.G.,Van Den Berg, S.,Weigelt, J.,Nordlund, P. (登録日: 2008-02-08, 公開日: 2008-03-11, 最終更新日: 2024-11-13)

主引用文献

Kursula, P.,Flodin, S.,Ehn, M.,Hammarstrom, M.,Schuler, H.,Nordlund, P.,Stenmark, P.
Structure of the Synthetase Domain of Human Ctp Synthetase, a Target for Anticancer Therapy.
Acta Crystallogr.,Sect.F, 62:613-, 2006

PubMed Abstract: 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.

PubMed: 16820675
DOI: 10.1107/S1744309106018136

実験手法

X-RAY DIFFRACTION (2.8 Å)