Duda David M, Schulman Brenda A
Department of Structural Biology, St. Jude Children's Research Hospital, 332 North Lauderdale Street, Memphis, Tennessee 38105, USA.
Mol Cell. 2005 Jun 10;18(6):612-4. doi: 10.1016/j.molcel.2005.05.017.
Structural and kinetic studies of a SUMORanGAP1-Ubc9-Nup358/RanBP2 complex (Reverter and Lima, 2005) provide the first high-resolution view of SUMO recognition by a SUMO binding motif and also reveal a novel mechanism for E3 ubiquitin-like protein ligases, with the Nup358/RanBP2 E3 teaming up with both SUMO and the E2 (Ubc9) to stimulate tagging.
对SUMORanGAP1-Ubc9-Nup358/RanBP2复合物的结构和动力学研究（Reverter和Lima，2005年）首次提供了SUMO结合基序识别SUMO的高分辨率视图，还揭示了E3泛素样蛋白连接酶的一种新机制，即Nup358/RanBP2 E3与SUMO和E2（Ubc9）协同作用以刺激标记。
