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Intrinsically disordered regions regulate the activities of ATP binding cassette transporters.
Biochimica et Biophysica Acta (BBA) - Biomembranes ( IF 3.4 ) Pub Date : 2020-01-20 , DOI: 10.1016/j.bbamem.2020.183202
Sarah C Bickers 1 , Jonathan S Sayewich 1 , Voula Kanelis 2
Affiliation  

ATP binding cassette (ABC) proteins are a large family of membrane proteins present in all kingdoms of life. These multi-domain proteins are comprised, at minimum, of two membrane-spanning domains (MSD1, MSD2) and two cytosolic nucleotide binding domains (NBD1, NBD2). ATP binding and hydrolysis at the NBDs enables ABC proteins to actively transport solutes across membranes, regulate activities of other proteins, or function as channels. Like most eukaryotic membrane proteins, ABC proteins contain intrinsically disordered regions (IDRs). These conformationally dynamic regions in ABC proteins possess residual structure, are sites of phosphorylation, and mediate protein-protein interactions. Here, we review the role of IDRs in regulating ABC protein activity.

中文翻译:

本质上无序的区域调节ATP结合盒转运蛋白的活性。

ATP结合盒(ABC)蛋白是存在于所有生命王国中的一大类膜蛋白。这些多结构域蛋白至少包含两个跨膜结构域(MSD1,MSD2)和两个胞质核苷酸结合结构域(NBD1,NBD2)。NBD处的ATP结合和水解使ABC蛋白能够主动地将溶质跨膜运输,调节其他蛋白的活性或充当通道。像大多数真核生物膜蛋白一样,ABC蛋白也包含固有的无序区(IDR)。ABC蛋白质中的这些构象动态区域具有残留结构,是磷酸化位点,并介导蛋白质-蛋白质相互作用。在这里,我们回顾了IDR在调节ABC蛋白活性中的作用。
更新日期:2020-01-21
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