De la Mora-Rey Teresa, Guenther Brian D, Finzel Barry C
Department of Medicinal Chemistry, University of Minnesota, 308 Harvard Street SE, 8-101 Weaver-Densford Hall, Minneapolis, MN 55455, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):723-9. doi: 10.1107/S1744309113015182. Epub 2013 Jun 27.
Mast/Orbit is a nonmotor microtubule-associated protein (MAP) present in Drosophila melanogaster that reportedly binds microtubules at the plus end and is essential for mitosis. Sequence analysis has shown that the N-terminal domain (Mast-M1) resembles TOG domains from the Dis1-TOG family of proteins and stands as a representative of one of the three subclasses of divergent TOG-like domains (TOGL1) that includes human CLASP1. The crystal structure of Mast-M1 has been determined at 2.0 Å resolution and provides the first detailed structural description of any TOG-like domain. The structure confirms that Mast-M1 adopts a similar fold to the previously described Dis1-TOG domains of microtubule-binding proteins. A comparison with three known TOG-domain structures from XMAP215/Dis1 family members exposes significant differences between Mast-M1 and other TOG-domain structures in key residues at the proposed tubulin-binding edge.
Mast/Orbit是一种存在于黑腹果蝇中的非运动性微管相关蛋白（MAP），据报道它在微管的正端结合微管，并且对有丝分裂至关重要。序列分析表明，N端结构域（Mast-M1）类似于Dis1-TOG蛋白家族的TOG结构域，是包括人类CLASP1在内的三种不同TOG样结构域（TOGL1）亚类之一的代表。Mast-M1的晶体结构已在2.0 Å分辨率下确定，首次对任何TOG样结构域进行了详细的结构描述。该结构证实Mast-M1采用了与先前描述的微管结合蛋白的Dis1-TOG结构域相似的折叠方式。与来自XMAP215/Dis1家族成员的三个已知TOG结构域结构进行比较，发现在拟议的微管蛋白结合边缘的关键残基上，Mast-M1与其他TOG结构域结构存在显著差异。
