CIDE-3的CIDE-N结构域的结晶及初步X射线晶体学研究
Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3.
作者信息
Lee Seung Mi, Park Hyun Ho
机构信息
School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1260-3. doi: 10.1107/S1744309113026444. Epub 2013 Oct 30.
The CIDE-3 protein plays a critical role in lipid metabolism by its involvement in lipid droplet formation. CIDE-3 contains two conserved cell-death-inducing DFF45-like effector (CIDE) domains (CIDE-N at the N-terminus and CIDE-C at the C-terminus) of ∼90 amino-acid residues that are involved in protein-protein interaction. In this study, the CIDE-N domain of CIDE-3 was purified and crystallized by the hanging-drop vapour-diffusion method and X-ray diffraction data were collected from the crystals to a resolution of 2.0 Å. The crystals were found to belong to space group P3(2), with unit-cell parameters a = b = 63.35, c = 37.60 Å, γ = 120°.
CIDE-3蛋白通过参与脂滴形成在脂质代谢中发挥关键作用。CIDE-3包含两个保守的细胞死亡诱导DFF45样效应子（CIDE）结构域（N端的CIDE-N和C端的CIDE-C），约90个氨基酸残基，参与蛋白质-蛋白质相互作用。在本研究中，通过悬滴气相扩散法纯化并结晶了CIDE-3的CIDE-N结构域，并从晶体中收集了X射线衍射数据，分辨率达到2.0 Å。发现晶体属于空间群P3(2)，晶胞参数a = b = 63.35，c = 37.60 Å，γ = 120°。
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