Thomas Jemima C, Green Judith L, Howson Ronald I, Simpson Peter, Moss David K, Martin Stephen R, Holder Anthony A, Cota Ernesto, Tate Edward W
Department of Chemistry, Imperial College London, Exhibition Rd., London, UK SW7 2AZ
Mol Biosyst. 2010 Mar;6(3):494-8. doi: 10.1039/b922093c. Epub 2010 Jan 27.
The myosin tail domain interacting protein-myosin A (MTIP-MyoA) protein complex is an essential element of the motor driving invasion of red blood cells by the Plasmodium species that cause malaria. Here we report the key determinants of binding at the MTIP/MyoA interface, and the first structural study on the complex in solution using protein NMR.
肌球蛋白尾部结构域相互作用蛋白-肌球蛋白A(MTIP-MyoA)蛋白复合物是导致疟疾的疟原虫物种驱动红细胞入侵的运动机制的关键要素。在此,我们报告了MTIP/MyoA界面结合的关键决定因素,并首次使用蛋白质核磁共振技术对溶液中的该复合物进行了结构研究。