Literature DB >> 23545662

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

Young Cheul Shin1, Eun Kyoung Seo, Ju Hong Jeon, Hyun Ho Park.   

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, γ = 120.00°.

Entities:  

Keywords:  PIST; Rab small G protein; membrane trafficking; oncogenic fusion

Mesh:

Substances:

Year:  2013        PMID: 23545662      PMCID: PMC3614181          DOI: 10.1107/S1744309113007082

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  25 in total

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  1 in total

1.  PIST (GOPC) modulates the oncogenic voltage-gated potassium channel KV10.1.

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  1 in total

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