1ufq

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(New page: 200px<br /> <applet load="1ufq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ufq, resolution 2.50&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of ligand-free human uridine-cytidine kinase 2'''<br />
'''Crystal structure of ligand-free human uridine-cytidine kinase 2'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1UFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UFQ OCA].
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1UFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1UFQ OCA].
==Reference==
==Reference==
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[[Category: Koizumi, K.]]
[[Category: Koizumi, K.]]
[[Category: Matsuda, A.]]
[[Category: Matsuda, A.]]
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[[Category: Suzuki, N.N.]]
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[[Category: Suzuki, N N.]]
[[Category: alpha/beta mononucleotide-binding hold]]
[[Category: alpha/beta mononucleotide-binding hold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:34:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:05 2008''

Revision as of 13:24, 21 February 2008


1ufq, resolution 2.50Å

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Crystal structure of ligand-free human uridine-cytidine kinase 2

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

1UFQ is a Single protein structure of sequence from Homo sapiens. Active as Uridine kinase, with EC number 2.7.1.48 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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