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2c5m

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==Overview==
==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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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==
==About this Structure==
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==Reference==
==Reference==
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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 Crystallograph Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):613-7. Epub 2006 Jun 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16820675 16820675]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16820675 16820675]
[[Category: CTP synthase]]
[[Category: CTP synthase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith, C.]]
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[[Category: Berg, S.Van.Den.]]
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[[Category: Berg, S Van Den.]]
[[Category: Berglund, H.]]
[[Category: Berglund, H.]]
[[Category: Edwards, A.]]
[[Category: Edwards, A.]]
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[[Category: Flodin, S.]]
[[Category: Flodin, S.]]
[[Category: Graslund, S.]]
[[Category: Graslund, S.]]
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[[Category: Hallberg, B.M.]]
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[[Category: Hallberg, B M.]]
[[Category: Hammarstrom, M.]]
[[Category: Hammarstrom, M.]]
[[Category: Kotenyova, T.]]
[[Category: Kotenyova, T.]]
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[[Category: Persson, C.]]
[[Category: Persson, C.]]
[[Category: Sagemark, J.]]
[[Category: Sagemark, J.]]
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[[Category: Schiavone, L.Holmberg.]]
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[[Category: Schiavone, L Holmberg.]]
[[Category: Schuler, H.]]
[[Category: Schuler, H.]]
[[Category: Stenmark, P.]]
[[Category: Stenmark, P.]]
[[Category: Sundstrom, M.]]
[[Category: Sundstrom, M.]]
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[[Category: Thorsell, A.G.]]
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[[Category: Thorsell, A G.]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: utp]]
[[Category: utp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:31:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:10 2008''

Revision as of 14:45, 21 February 2008


2c5m, resolution 2.8Å

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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

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