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Arrestins: structural disorder creates rich functionality

机译：Arrestins：结构紊乱产生丰富的功能

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摘要

Arrestins are soluble relatively small 44–46 kDa proteins that specifically bind hundreds of active phosphorylated GPCRs and dozens of non-receptor partners. There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound. Recent evidence suggests that conformational flexibility in every functional state is the defining characteristic of arrestins. Flexibility, or plasticity, of proteins is often described as structural disorder, in contrast to the fixed conformational order observed in high-resolution crystal structures. However, protein-protein interactions often involve highly flexible elements that can assume many distinct conformations upon binding to different partners. Existing evidence suggests that arrestins are no exception to this rule: their flexibility is necessary for functional versatility. The data on arrestins and many other multi-functional proteins indicate that in many cases, “order” might be artificially imposed by highly non-physiological crystallization conditions and/or crystal packing forces. In contrast, conformational flexibility (and its extreme case, intrinsic disorder) is a more natural state of proteins, representing true biological order that underlies their physiologically relevant functions.
机译：抑制蛋白是可溶的相对较小的44-46 kDa蛋白，可特异性结合数百种活性磷酸化GPCR和数十种非受体伴侣。有结合伴侣显示出对每种已知的抑制蛋白构象的偏爱：游离，受体结合和微管结合。最近的证据表明，每个功能状态的构象柔韧性是抑制蛋白的定义特征。与高分辨率晶体结构中观察到的固定构象顺序相反，蛋白质的柔韧性或可塑性通常被描述为结构紊乱。但是，蛋白质间相互作用通常涉及高度灵活的元素，这些元素在与不同的伴侣结合后可以呈现许多不同的构象。现有证据表明，抑制蛋白也不例外，其规则是其功能多样性所必需的。关于抑制蛋白和许多其他多功能蛋白质的数据表明，在许多情况下，“顺序”可能是由高度非生理的结晶条件和/或晶体堆积力人工施加的。相反，构象灵活性（及其极端情况，内在障碍）是蛋白质的一种更自然的状态，代表了构成其生理相关功能基础的真实生物学顺序。

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