VIB Structural Biology Research Center (SBRC), Brussels, Belgium; Vrije Universiteit Brussel, Brussels, Belgium; Institute of Enzymology, Research Centre for Natural Sciences of the Hungarian Academy of Sciences, Budapest, Hungary.
Institute of Enzymology, Research Centre for Natural Sciences of the Hungarian Academy of Sciences, Budapest, Hungary.
Curr Opin Struct Biol. 2015 Dec;35:49-59. doi: 10.1016/j.sbi.2015.08.009. Epub 2015 Sep 21.
Intrinsically disordered proteins or regions of proteins (IDPs/IDRs) most often function through protein-protein interactions, when they permanently or transiently bind partner molecules with diverse functional consequences. There is a rapid advance in our understanding of the ensuing functional modes, obtained from describing atomic details of individual complexes, proteome-wide studies of interactomes and characterizing loosely assembled hydrogels and tightly packed amyloids. Here we briefly survey the most important recent methodological developments and structural-functional observations, with the aim of increasing the general appreciation of IDPs/IDRs as 'interaction specialists'.
无规蛋白或蛋白区域(IDPs/IDRs)通常通过蛋白-蛋白相互作用发挥功能,当它们与具有不同功能后果的伴侣分子永久或暂时结合时。我们对随之而来的功能模式的理解正在迅速推进,这些模式是通过描述单个复合物的原子细节、对相互作用组的蛋白质组范围研究以及对松散组装的水凝胶和紧密堆积的淀粉样蛋白进行特征描述而获得的。在这里,我们简要综述了最近最重要的方法学发展和结构-功能观察,旨在提高人们对 IDPs/IDRs 作为“相互作用专家”的普遍认识。