Mohan P M Krishna, Hosur Ramakrishna V
Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India.
J Biosci. 2009 Sep;34(3):465-79. doi: 10.1007/s12038-009-0052-0.
The detailed characterization of the structure, dynamics and folding process of a protein is crucial for understanding the biological functions it performs. Modern biophysical and nuclear magnetic resonance (NMR) techniques have provided a way to obtain accurate structural and thermodynamic information on various species populated on the energy landscape of a given protein. In this context, we review here the structure-function-folding relationship of an important protein, namely, dynein light chain protein (DLC8). DLC8, the smallest subunit of the dynein motor complex, acts as a cargo adaptor. The protein exists as a dimer under physiological conditions and dissociates into a pure monomer below pH 4. Cargo binding occurs at the dimer interface. Dimer stability and relay of perturbations through the dimer interface are anticipated to be playing crucial roles in the variety of functions the protein performs. NMR investigations have provided great insights into these aspects of DLC8 in recent years.
蛋白质结构、动力学和折叠过程的详细表征对于理解其执行的生物学功能至关重要。现代生物物理和核磁共振（NMR）技术提供了一种方法，可获取给定蛋白质能量景观上各种物种的准确结构和热力学信息。在此背景下，我们在此回顾一种重要蛋白质，即动力蛋白轻链蛋白（DLC8）的结构 - 功能 - 折叠关系。DLC8是动力蛋白运动复合体的最小亚基，作为货物适配器发挥作用。该蛋白在生理条件下以二聚体形式存在，在pH值低于4时解离为纯单体。货物结合发生在二聚体界面。预计二聚体稳定性以及通过二聚体界面传递的扰动在该蛋白执行的各种功能中起着关键作用。近年来，NMR研究为DLC8的这些方面提供了深入见解。
