Open AccessCrystallization and preliminary X‐ray diffraction analysis of human dipeptidyl peptidase 10 (DPPY), a component of voltage‐gated potassium channels
Author(s) -
Bezerra Gustavo Arruda,
Dobrovetsky Elena,
Seitova Alma,
DhePaga Sirano,
Gruber Karl
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111055230
Subject(s) - crystallization , potassium , materials science , diffraction , component (thermodynamics) , x ray , dipeptidyl peptidase , crystallography , x ray crystallography , analytical chemistry (journal) , chemistry , chromatography , optics , enzyme , biochemistry , physics , thermodynamics , metallurgy , organic chemistry
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 purified via His‐tag affinity and size‐exclusion chromatography. Crystals obtained by the sitting‐drop method were orthorhombic, belonging to space group P 2 1 2 1 2 1 with unit‐cell parameters a = 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.