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1ufq
From Proteopedia
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[[Image:1ufq.gif|left|200px]] | [[Image:1ufq.gif|left|200px]] | ||
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'''Crystal structure of ligand-free human uridine-cytidine kinase 2''' | '''Crystal structure of ligand-free human uridine-cytidine kinase 2''' | ||
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[[Category: Matsuda, A.]] | [[Category: Matsuda, A.]] | ||
[[Category: Suzuki, N N.]] | [[Category: Suzuki, N N.]] | ||
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Revision as of 08:09, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 11:09:39 2008
