Roman Noelia, Kirkby Brenda, Marfori Mary, Kobe Bostjan, Forwood Jade K
School of Biomedical Sciences, Charles Sturt University, Wagga Wagga, NSW 2650, Australia.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):625-8. doi: 10.1107/S1744309109016820. Epub 2009 May 22.
The transport of macromolecules across the nuclear envelope is an essential eukaryotic process that enables proteins such as transcription factors, polymerases and histones to gain access to the genetic material contained within the nucleus. Importin-beta plays a central role in the nucleocytoplasmic transport process, mediating nuclear import through a range of interactions with cytoplasmic, nuclear and nuclear pore proteins such as importin-alpha, Ran, nucleoporins and various cargo molecules. The unliganded form of the full-length yeast importin-beta has been expressed and crystallized. The crystals were obtained by vapour diffusion at pH 6.5 and 290 K. The crystals belonged to space group P2(1) (unit-cell parameters a = 58.17, b = 127.25, c = 68.52 A, beta = 102.23). One molecule is expected in the asymmetric unit. The crystals diffracted to 2.4 A resolution using a laboratory X-ray source and were suitable for crystal structure determination.
大分子穿过核膜的运输是真核生物的一个基本过程，它使转录因子、聚合酶和组蛋白等蛋白质能够接触到细胞核内的遗传物质。输入蛋白β在核质运输过程中起着核心作用，通过与细胞质、细胞核和核孔蛋白（如输入蛋白α、Ran、核孔蛋白和各种货物分子）的一系列相互作用介导核输入。全长酵母输入蛋白β的未结合配体形式已被表达并结晶。晶体通过在pH 6.5和290 K下的气相扩散获得。晶体属于空间群P2(1)（晶胞参数a = 58.17，b = 127.25，c = 68.52 Å，β = 102.23）。不对称单元中预计有一个分子。使用实验室X射线源，晶体衍射到2.4 Å分辨率，适合进行晶体结构测定。
