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

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.