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Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST.

ABSTRACT: PIST [PDZ (PSD-95, Discs-large and ZO-1) protein interacting specifically with TC10] functions as a regulator of membrane trafficking with Rab6A. Recently, the involvement of the fusion of PIST with ROS1 in cancer development has been identified. In this study, the coiled-coil domain of PIST, which is the domain responsible for interaction with Rab6A and fusion with ROS1, corresponding to amino acids 29-133, was overexpressed in Escherichia coli using engineered C-terminal His tags. The coiled-coil domain of PIST was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 4.0 Å from a crystal belonging to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 85.19, c = 240.09 Å, ? = 120.00°.

SUBMITTER: Shin YC

PROVIDER: S-EPMC3614181 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST.

Shin Young Cheul YC Seo Eun Kyoung EK Jeon Ju Hong JH Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology and crystallization communications 20130329 Pt 4

PIST [PDZ (PSD-95, Discs-large and ZO-1) protein interacting specifically with TC10] functions as a regulator of membrane trafficking with Rab6A. Recently, the involvement of the fusion of PIST with ROS1 in cancer development has been identified. In this study, the coiled-coil domain of PIST, which is the domain responsible for interaction with Rab6A and fusion with ROS1, corresponding to amino acids 29-133, was overexpressed in Escherichia coli using engineered C-terminal His tags. The coiled-c ...[more]

PMID: 23545662

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