Crystallography of cargo-mediated activation mechanism of molecular motor proteins, kinesin superfamily members KIF5 and KIF13B

分子运动蛋白、驱动蛋白超家族成员 KIF5 和 KIF13B 的货物介导激活机制的晶体学

• 批准号: 371633-2009
• 负责人: Park, HeeWon
• 金额: $ 2.33万
• 依托单位: University of Toronto
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2011
• 资助国家: 加拿大
• 起止时间: 2011-01-01 至 2012-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=483664
• 关键词: Crystallography; cargo; mediated; activation; mechanism

Kinesins are molecular motors that share a common structural core with myosins and G proteins and play diverse roles in organelle transport, cell division, and cell movement. Kinesin motors use the chemical energy derived from the hydrolysis of adenosine tri-phosphate to generate force for a unidirectional movement along the microtubule highway and transport cargoes (vesicles, protein complexes, RNAs and mitochondria). Regulation of kinesin motors is important because a constantly active motor would consume futile adenosine tri-phosphate and move to the tips of microtubules without loaded cargoes. Both Kinesin-1 and KIF13B cycle between two conformations: the folded, inhibited state and the extended, activated state. The proposed studies will give a first look at the structures of the cargo binding domains and provide a basis for explaining how kinesin is regulated by the cargo binding domains.

驱动蛋白是分子马达，与肌球蛋白和 G 蛋白具有共同的结构核心，在细胞器运输、细胞分裂和细胞运动中发挥着不同的作用。驱动蛋白马达利用三磷酸腺苷水解产生的化学能产生沿着微管高速公路单向运动的力并运输货物（囊泡、蛋白质复合物、RNA 和线粒体）。驱动蛋白马达的调节很重要，因为持续活跃的马达会消耗无用的三磷酸腺苷，并在没有装载货物的情况下移动到微管的尖端。 Kinesin-1 和 KIF13B 都在两种构象之间循环：折叠、抑制状态和延伸、激活状态。 拟议的研究将首先观察货物结合域的结构，并为解释货物结合域如何调节驱动蛋白提供基础。