1udw

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[[Image:1udw.gif|left|200px]]<br /><applet load="1udw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1udw.gif|left|200px]]
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caption="1udw, resolution 2.60&Aring;" />
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'''Crystal structure of human uridine-cytidine kinase 2 complexed with a feedback-inhibitor, CTP'''<br />
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{{Structure
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|PDB= 1udw |SIZE=350|CAPTION= <scene name='initialview01'>1udw</scene>, resolution 2.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48]
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|GENE=
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}}
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'''Crystal structure of human uridine-cytidine kinase 2 complexed with a feedback-inhibitor, CTP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CTP:'>CTP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDW OCA].
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1UDW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDW OCA].
==Reference==
==Reference==
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Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase., Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F, Structure. 2004 May;12(5):751-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15130468 15130468]
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Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase., Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F, Structure. 2004 May;12(5):751-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15130468 15130468]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: alpha/beta mononucleotide-binding hold]]
[[Category: alpha/beta mononucleotide-binding hold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:30:43 2008''

Revision as of 12:30, 20 March 2008


PDB ID 1udw

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
Activity: Uridine kinase, with EC number 2.7.1.48
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human uridine-cytidine kinase 2 complexed with a feedback-inhibitor, CTP


Overview

Uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine and cytidine and activates pharmacological ribonucleoside analogs. Here we present the crystal structures of human UCK alone and in complexes with a substrate, cytidine, a feedback inhibitor, CTP or UTP, and with phosphorylation products, CMP and ADP, respectively. Free UCK takes an alpha/beta mononucleotide binding fold and exists as a homotetramer with 222 symmetry. Upon inhibitor binding, one loop region was loosened, causing the UCK tetramer to be distorted. Upon cytidine binding, a large induced fit was observed at the uridine/cytidine binding site, which endows UCK with a strict specificity for pyrimidine ribonucleosides. The first UCK structure provided the structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase, which give clues for the design of novel antitumor and antiviral ribonucleoside analogs that inhibit RNA synthesis.

About this Structure

1UDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase., Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F, Structure. 2004 May;12(5):751-64. PMID:15130468

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