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Crystal structure of human MTH1 and the 8-oxo-dGMP product complex
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
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2011 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 585, no 16, 2617-2621 p.Article in journal (Refereed) Published
Abstract [en]

MTH1 hydrolyzes oxidized nucleotide triphosphates, thereby preventing them from being incorporated into DNA. We here present the structures of human MTH1 (1.9 angstrom) and its complex with the product 8-oxo-dGMP (1.8 angstrom). Unexpectedly MTH1 binds the nucleotide in the anti conformation with no direct interaction between the 8-oxo group and the protein. We suggest that the specificity depends on the stabilization of an enol tautomer of the 8-oxo form of dGTP. The binding of the product induces no major structural changes. The structures reveal the mode of nucleotide binding in MTH1 and provide the structural basis for inhibitor design.

Place, publisher, year, edition, pages
2011. Vol. 585, no 16, 2617-2621 p.
Keyword [en]
MTH1, MutT, Oxidative damage, 8-oxo-dGTPase, NUDT1, 8-oxo-dGTP, Tautomer
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:su:diva-68308DOI: 10.1016/j.febslet.2011.07.017ISI: 000293826300012OAI: oai:DiVA.org:su-68308DiVA: diva2:477508
Funder
Swedish Research CouncilSwedish Foundation for Strategic Research The Wenner-Gren FoundationSwedish Cancer Society
Note

authorCount :7

Available from: 2012-01-13 Created: 2012-01-03 Last updated: 2017-12-08Bibliographically approved

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Svensson, Linda M.Jemth, Ann-SofieDesroses, MatthieuLoseva, OlgaHelleday, ThomasStenmark, Pål
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Department of Biochemistry and BiophysicsDepartment of Genetics, Microbiology and Toxicology
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