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Visualization of transient encounter complexes in protein-protein association

机译：蛋白质-蛋白质缔合中瞬时相遇复合物的可视化

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摘要

Kinetic data on a number of protein - protein associations have provided evidence for the initial formation of a pre- equilibrium encounter complex that subsequently relaxes to the final stereospecific complex (1). Site- directed mutagenesis(2 - 4) and brownian dynamics simulations(5 - 7) have suggested that the rate of association can be modulated by perturbations in charge distribution outside the direct interaction surfaces. Furthermore, rate enhancement through non- specific binding may occur by either a reduction in dimensionality(8) or the presence of a short- range, non- specific attractive potential(9). Here, using paramagnetic relaxation enhancement, we directly demonstrate the existence and visualize the distribution of an ensemble of transient, non- specific encounter complexes under equilibrium conditions for a relatively weak protein - protein complex between the amino- terminal domain of enzyme I and the phosphocarrier protein HPr. Neither the stereospecific complex(10) alone nor any single alternative conformation can account fully for the intermolecular paramagnetic relaxation enhancement data. Restrained rigid- body simulated annealing refinement against the paramagnetic relaxation enhancement data enables us to obtain an atomic probability distribution map of the non- specific encounter complex ensemble that qualitatively correlates with the electrostatic surface potentials on the interacting proteins. Qualitatively similar results are presented for two other protein - protein complexes.
机译：许多蛋白质-蛋白质缔合的动力学数据为初步形成平衡前复合物的形成提供了证据，该复合物随后松弛为最终的立体特异性复合物（1）。定点诱变（2-4）和布朗动力学模拟（5-7）表明，缔合速率可以通过直接相互作用表面外部电荷分布的扰动来调节。此外，通过降低尺寸（8）或存在短距离的非特异性吸引力（9），可以通过非特异性结合提高速率。在这里，使用顺磁弛豫增强，我们直接证明了平衡状态下瞬态，非特异性相遇复合体的存在，并可视化了酶I的氨基末端结构域与磷酸载体之间相对较弱的蛋白质-蛋白质复合体的平衡分布蛋白HPr。单独的立体定向复合物（10）或任何单一的替代构型都不能完全解释分子间顺磁弛豫增强数据。对顺磁弛豫增强数据进行约束的刚体模拟退火优化使我们能够获得与相互作用蛋白质上的静电表面电势定性相关的非特异性相遇复合体集合的原子概率分布图。对于其他两种蛋白质-蛋白质复合物，在质量上也有相似的结果。

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