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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2(68), p. 214-217, 2012

DOI: 10.1107/s1744309111055230

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Crystallization and preliminary X-ray diffraction analysis of human dipeptidyl peptidase 10 (DPPY), a component of voltage-gated potassium channels

This paper is available in a repository.
This paper is available in a repository.

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Abstract

Dipeptidyl peptidase 10 (DPP10, DPPY) is an inactive peptidase associated with voltage-gated potassium channels, acting as a modulator of their electrophysiological properties, cell-surface expression and subcellular localization. Because potassium channels are important disease targets, biochemical and structural characterization of their interaction partners was sought. DPP10 was cloned and expressed using an insect-cell system and the protein was purifiedvia His-tag affinity and size-exclusion chromatography. Crystals obtained by the sitting-drop method were orthorhombic, belonging to space groupP212121with unit-cell parametersa= 80.91,b= 143.73,c= 176.25 Å. A single solution with two molecules in the asymmetric unit was found using the structure of DPP6 (also called DPPX; PDB entry 1xfd) as the search model in a molecular replacement protocol.