@inbook{795879f4be4b4859b11a53a9877da7f1,
title = "Crystallization of Nuclear Export Signals or Small-Molecule Inhibitors Bound to Nuclear Exporter CRM1",
abstract = "The Karyopherin protein CRM1 or XPO1 is the major nuclear export receptor that regulates nuclear exit of thousands of macromolecules in the cell. CRM1 recognizes protein cargoes by binding to their 8–15 residue-long nuclear export signals (NESs). A ternary CRM1–Ran–RanBP1 complex engineered to be suitable for crystallization has enabled structure determination by X-ray crystallography of CRM1 bound to many NES peptides and small-molecule inhibitors. Here, we present a protocol for the purification of the individual proteins, formation of the ternary CRM1–Ran–RanBP1 complex and crystallization of this complex for X-ray crystallography.",
keywords = "CRM1, KPT, Leptomycin B, LMB, NES, Nuclear export signals, SINE, X-ray crystallography, XPO1",
author = "Fung, {Ho Yee Joyce} and Chook, {Yuh Min}",
note = "Funding Information: We would like to thank Jordan Baumhardt for assisting in the completion of the manuscript. This work is funded by the Cancer Prevention Research Institute of Texas (CPRIT) Grants RP180410 and RP170170 (Y.M.C.), Welch Foundation Grant I-1532 (Y.M. C), NIGMS of NIH under Award R01GM069909 (Y.M.C.), the Mabel and Alfred Gilman Chair for Molecular Pharmacology (Y.M. C.), and the Eugene McDermott Scholar in Biomedical Research (Y.M.C.). Publisher Copyright: {\textcopyright} 2022, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2022",
doi = "10.1007/978-1-0716-2337-4_19",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "285--297",
booktitle = "Methods in Molecular Biology",
}