An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor

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Title
An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor
Author(s)
Do-Hyoung Kim; A Wright; Kyou Hoon Han
Bibliographic Citation
BMB Reports, vol. 50, no. 10, pp. 522-527
Publication Year
2017
Abstract
A large number of transcriptional activation domains (TADs) are intrinsically unstructured, meaning they are devoid of a three-dimensional structure. The fact that these TADs are transcriptionally active without forming a 3-D structure raises the question of what features in these domains enable them to function. One of two TADs in human glucocorticoid receptor (hGR) is located at its N-terminus and is responsible for ~70% of the transcriptional activity of hGR. This 58-residue intrinsically- disordered TAD, named tau1c in an earlier study, was shown to form three helices under trifluoroethanol, which might be important for its activity. We carried out heteronuclear multi-dimensional NMR experiments on hGR tau1c in a more physiological aqueous buffer solution and found that it forms three helices that are ~30% pre-populated. Since pre-populated helices in several TADs were shown to be key elements for transcriptional activity, the three pre-formed helices in hGR tau1c delineated in this study should be critical determinants of the transcriptional activity of hGR. The presence of prestructured helices in hGR tau1c strongly suggests that the existence of pre-structured motifs in target-unbound TADs is a very broad phenomenon.
Keyword
Human glucocorticoid receptor (hGR)Intrinsically disordered protein (IDP)Nuclear magnetic resonance (NMR)Prestructured motif (PreSMo)
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5483/BMBRep.2017.50.10.152
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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