如何唤醒你的纳米机器：通过配体相互作用实现粘着斑激酶的位点特异性激活。
How to awaken your nanomachines: Site-specific activation of focal adhesion kinases through ligand interactions.
作者信息
Walkiewicz Katarzyna W, Girault Jean-Antoine, Arold Stefan T
机构信息
King Abdullah University of Science and Technology (KAUST), Division of Biological and Environmental Sciences and Engineering, Computational Bioscience Research Center (CBRC), Thuwal, Saudi Arabia.
Inserm, UMR-S 839, F-75005 Paris, France; Université Pierre & Marie Curie (UPMC), Sorbonne Universités, F-75005 Paris, France; Institut du Fer à Moulin, F-75005 Paris, France.
出版信息
Prog Biophys Mol Biol. 2015 Oct;119(1):60-71. doi: 10.1016/j.pbiomolbio.2015.06.001. Epub 2015 Jun 17.
The focal adhesion kinase (FAK) and the related protein-tyrosine kinase 2-beta (Pyk2) are highly versatile multidomain scaffolds central to cell adhesion, migration, and survival. Due to their key role in cancer metastasis, understanding and inhibiting their functions are important for the development of targeted therapy. Because FAK and Pyk2 are involved in many different cellular functions, designing drugs with partial and function-specific inhibitory effects would be desirable. Here, we summarise recent progress in understanding the structural mechanism of how the tug-of-war between intramolecular and intermolecular interactions allows these protein 'nanomachines' to become activated in a site-specific manner.
粘着斑激酶（FAK）和相关蛋白酪氨酸激酶2-β（Pyk2）是高度通用的多结构域支架蛋白，在细胞粘附、迁移和存活中起核心作用。由于它们在癌症转移中起关键作用，因此了解和抑制它们的功能对于靶向治疗的发展至关重要。由于FAK和Pyk2参与许多不同的细胞功能，设计具有部分和功能特异性抑制作用的药物将是理想的。在这里，我们总结了最近在理解分子内和分子间相互作用之间的拔河如何使这些蛋白质“纳米机器”以位点特异性方式激活的结构机制方面取得的进展。
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