Crystallization and preliminary X-ray crystallographic studies of transportin 1 in complex with nucleocytoplasmic shuttling and nuclear localization fragments.

ABSTRACT: Nucleocytoplasmic transport of proteins with molar masses of larger than 60,000 is mediated by transport receptors. The transport receptor transportin1 (Trn1) transports various kinds of RNA-binding proteins such as JKTBP, hnRNP D and TAP. Trn1 was successfully cocrystallized with nucleocytoplasmic shuttling fragments of JKTBP and hnRNP D and a nuclear localization fragment of TAP. The crystal of the Trn1-JKTBP fragment complex belongs to space group P2(1)2(1)2, with unit-cell parameters a = 131.5, b =171.5, c = 68.2 angstroms. The crystals of Trn1 in complex with hnRNP D and TAP fragments are orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 69.1, b = 119.1, c = 151.1 angstroms and a = 69.0, b = 119.1, c = 146.0 angstroms, respectively. The crystals diffracted to beyond 3.0, 3.2 and 2.4 angstroms resolution, respectively, using synchrotron radiation at SPring-8.

SUBMITTER: Imasaki T 

PROVIDER: S-EPMC2242924 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature