2vo1

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{{STRUCTURE_2vo1| PDB=2vo1 | SCENE= }}
{{STRUCTURE_2vo1| PDB=2vo1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE'''
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===CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16820675}}
==About this Structure==
==About this Structure==
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[[Category: Pyrimidine biosynthesis]]
[[Category: Pyrimidine biosynthesis]]
[[Category: Utp]]
[[Category: Utp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:46:57 2008''

Revision as of 14:47, 28 July 2008

Image:2vo1.png

Template:STRUCTURE 2vo1

CRYSTAL STRUCTURE OF THE SYNTHETASE DOMAIN OF HUMAN CTP SYNTHETASE

Template:ABSTRACT PUBMED 16820675

About this Structure

2VO1 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2c5m. 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

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