Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, CA 95064, USA.
Proteins. 2011 Jun;79(6):2010-4. doi: 10.1002/prot.23007. Epub 2011 Apr 12.
The retinoblastoma protein (Rb) regulates cell proliferation through its association with E2F transcription factors and other proteins. The Rb “pocket” domain primarily facilitates protein-protein interactions, and several structures of the pocket bound to E2F and tumorigenic viral proteins have been reported. We report here the first crystal structure of the pocket domain without bound ligand. We find that ligand association results in observable structural changes at the binding sites but no significant changes to the overall conformation of the domain. These data support models for regulation of Rb-E2F binding that do not require considerable structural changes in the pocket domain.
视网膜母细胞瘤蛋白（Rb）通过与 E2F 转录因子和其他蛋白的结合来调节细胞增殖。Rb“口袋”结构域主要促进蛋白-蛋白相互作用，已有多个结合 E2F 和致瘤性病毒蛋白的口袋结构的报道。我们在此报告第一个无配体结合的口袋结构域的晶体结构。我们发现配体结合导致结合部位的结构变化可观察到，但对该结构域的整体构象没有显著影响。这些数据支持了不需要口袋结构域发生显著结构变化即可调节 Rb-E2F 结合的模型。
