title: 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, γ = 120.00°.
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.
authors.forename: Young Cheul
authors.initials: YC
authors.lastname: Shin
authors.forename: Eun Kyoung
authors.initials: EK
authors.lastname: Seo
authors.forename: Ju Hong
authors.initials: JH
authors.lastname: Jeon
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D000077614:Golgi Matrix Proteins; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D026901:Membrane Transport Proteins
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; C434484:GOPC protein, human; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins
keywords: PIST; Rab small G protein; membrane trafficking; oncogenic fusion
references.citation: J Biol Chem. 2003 Nov 14;278(46):46046-51
references.pmid: 12954645
references.citation: J Biol Chem. 2009 Jan 30;284(5):2628-2635
references.pmid: 19019823
references.citation: Nature. 1990 Jun 7;345(6275):553-6
references.pmid: 2112230
references.citation: J Biol Chem. 2013 Feb 15;288(7):5114-26
references.pmid: 23243314
references.citation: Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):916-21
references.pmid: 12538861
references.citation: J Biol Chem. 2002 Feb 1;277(5):3520-9
references.pmid: 11707463
references.citation: PLoS One. 2011;6(12):e28250
references.pmid: 22163003
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Nat Cell Biol. 2002 Dec;4(12):986-92
references.pmid: 12447383
references.citation: Biochem Biophys Res Commun. 2001 Aug 31;286(4):771-8
references.pmid: 11520064
references.citation: J Cell Sci. 1992 Nov;103 ( Pt 3):785-96
references.pmid: 1478971
references.citation: Nat Rev Mol Cell Biol. 2009 Aug;10(8):513-25
references.pmid: 19603039
references.citation: J Biol Chem. 2001 Aug 3;276(31):29456-65
references.pmid: 11384996
references.citation: Biochem Biophys Res Commun. 2001 Jan 19;280(2):541-7
references.pmid: 11162552
references.citation: Traffic. 2002 Apr;3(4):289-97
references.pmid: 11929610
references.citation: Curr Biol. 2002 Oct 15;12(20):1792-5
references.pmid: 12401177
references.citation: PLoS One. 2011 Mar 21;6(3):e18080
references.pmid: 21445309
references.citation: Mol Biol Cell. 2000 Nov;11(11):3819-33
references.pmid: 11071909
references.citation: Nat Commun. 2012 Feb 07;3:662
references.pmid: 22314358
references.citation: Clin Cancer Res. 2012 Dec 15;18(24):6599-608
references.pmid: 23052255
references.citation: FASEB J. 1996 Apr;10(5):625-30
references.pmid: 8621061
references.citation: J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
references.pmid: 19461840
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: Nat Cell Biol. 1999 May;1(1):E17-22
references.pmid: 10559876
references.citation: Science. 1998 Jan 23;279(5350):580-5
references.pmid: 9438855