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1udw

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Revision as of 14:10, 25 December 2019

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

Structural highlights

1udw is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Uridine kinase, with EC number 2.7.1.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UCK2_HUMAN] Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F. Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. PMID:15130468 doi:10.1016/j.str.2004.02.038

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1udw"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human uridine-cytidine kinase 2 complexed with a feedback-inhibitor, CTP==
-<StructureSection load='1udw' size='340' side='right' caption='[[1udw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='1udw' size='340' side='right'caption='[[1udw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1udw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UDW FirstGlance]. <br>
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Uridine kinase]]
 [[Category: Fukushima, M]]

1udw

From Proteopedia

Revision as of 14:10, 25 December 2019

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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