Multiple hTAFII31-binding motifs in the intrinsically unfolded transcriptional activation domain of VP16

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Title
Multiple hTAFII31-binding motifs in the intrinsically unfolded transcriptional activation domain of VP16
Author(s)
D H Kim; Si-Hyung Lee; Ki Hoon Nam; Seung-Wook Chi; I Chang; Kyou Hoon Han
Bibliographic Citation
BMB Reports, vol. 42, no. 7, pp. 411-417
Publication Year
2009
Abstract
Transcriptional activation domain (TAD) in virion protein 16 (VP16) of herpes simplex virus does not have any globular structure, yet exhibits a potent transcriptional activity. In order to probe the structural basis for the transcriptional activity of VP16 TAD, we have used NMR spectroscopy to investigate its detailed structural features. Results show that an unbound VP16 TAD is not merely “unstructured” but contains four short motifs (residues 424-433, 442-446, 465-467 and 472-479) with transient structural order. Pre-structured motifs in other intrinsically unfolded proteins (IUPs) were shown to be critically involved in target protein binding. The 472-479 motif was previously shown to bind to hTAFII31, whereas the hTAFII31-binding ability of other motifs found in this study has not been addressed. The VP16 TAD represents another IUP whose prestructured motifs mediate promiscuous binding to various target proteins.
Keyword
Herpes simplex virushTAFII31Intrinsically unfolded proteinNMRTranscriptional activation domainVP16
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/BMBRep.2009.42.7.411
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
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