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Expression, Purification, Crystallization, and Preliminary X-Ray Analysis of the Human UDP-Glucose Dehydrogenase

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UDP-glucose dehydrogenase (UGDH) catalyzes the synthesis of UDP-glucuronic acid from UDP-glucose resulting in the formation of proteoglycans that are involved in promoting normal cellular growth and migration. Overproduction of proteoglycans has been implicated in the progression of certain epithelial cancers. Here, human UGDH (hUGDH) was purified and crystallized from a solution of 0.2 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, and 21% PEG 8000. Diffraction data were collected to a resolution of 2.8 Å . The crystal belongs to the orthorhombic space group P212121 with unit-cell parameters a = 173.25, b = 191.16, c = 225.94 Å , and α = β = γ = 90.0 °. Based on preliminary analysis of the diffraction data, we propose that the biological unit of hUGDH is a tetramer.

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Keywords: GMDH; UDP-glucose; UDP-glucuronic acid; UGDH; crystallization

Document Type: Research Article

Affiliations: Department of Biochemistry and Molecular Biology, cDepartment of Physiology, dResearch Institute for Biomacromolecules, University of Ulsan College of Medicine, Seoul 138-736, South Korea.

Publication date: 01 August 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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