García-Morales Abigail, Pulido Nancy O, Balleza Daniel
Unidad de Investigación y Desarrollo en Alimentos, Instituto Tecnológico de Veracruz, Tecnológico Nacional de México, Calz. Miguel Angel de Quevedo 2779 Col Formando Hogar, 91897, Veracruz, Ver, Mexico.
Escuela de Ingeniería y Ciencias, Instituto Tecnológico y de Estudios Superiores de Monterrey, Cuernavaca, Mexico.
Eur Biophys J. 2024 Feb;53(1-2):77-90. doi: 10.1007/s00249-023-01682-9. Epub 2023 Sep 30.
How a protein propagates the conformational changes throughout its structure remains largely unknown. In thermosensitive TRP channels, this allosteric communication is triggered by ligand interaction or in response to temperature changes. Because dynamic allostery suggests a dynamic role of disordered regions, in this work we set out to thoroughly evaluate these regions in six thermosensitive TRP channels. Thus, by contrasting the intrinsic flexibility of the transmembrane region as a function of the degree of disorder in those proteins, we discovered several residues that do not show a direct correlation in both parameters. This kind of structural discrepancy revealed residues that are either reported to be dynamic, functionally relevant or are involved in signal propagation and probably part of allosteric networks. These discrepant, potentially dynamic regions are not exclusive of TRP channels, as this same correlation was found in the Kv Shaker channel.
蛋白质如何在其整个结构中传播构象变化在很大程度上仍然未知。在热敏性瞬时受体电位（TRP）通道中，这种变构通讯是由配体相互作用或对温度变化的响应触发的。由于动态变构表明无序区域具有动态作用，因此在这项工作中，我们着手全面评估六个热敏性TRP通道中的这些区域。因此，通过对比跨膜区域的固有灵活性与这些蛋白质中无序程度的函数关系，我们发现了几个在这两个参数中没有直接相关性的残基。这种结构差异揭示了那些据报道具有动态性、功能相关性或参与信号传播且可能是变构网络一部分的残基。这些存在差异的、潜在的动态区域并非TRP通道所特有，因为在Kv Shaker通道中也发现了同样的相关性。
