Pan Dongqing, Matsuura Yoshiyuki
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):386-92. doi: 10.1107/S1744309112007178. Epub 2012 Mar 27.
In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.
在真核生物中，被称为雷帕霉素靶蛋白复合物1（TORC1）和雷帕霉素靶蛋白复合物2（TORC2）的多蛋白复合物作为细胞生长、代谢和衰老的主要调节因子发挥作用。酿酒酵母TORC2组分Avo1的C末端结构域是TORC2定位于质膜所必需的，并且对酵母的生存能力至关重要。已确定Avo1的C末端结构域及其人类同源物Sin1的X射线晶体结构。这些结构表明，Avo1和Sin1的C末端均具有普列克底物蛋白同源（PH）结构域折叠。与已知的PH结构域结构进行比较，提示了一个磷酸肌醇的假定结合位点。
