Open AccessMultiple hTAFII31-binding motifs in the intrinsically unfolded transcriptional activation domain of VP16
Author(s) -
Do Hyoung Kim,
Si Hyung Lee,
Ki Hoon Nam,
Seung Wook,
Ik Soo Chang,
KyouHoon Han
Publication year - 2009
Publication title -
bmb reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.511
H-Index - 77
eISSN - 1976-670X
pISSN - 1976-6696
DOI - 10.5483/bmbrep.2009.42.7.411
Subject(s) - intrinsically disordered proteins , computational biology , chemistry , herpes simplex virus , nuclear magnetic resonance spectroscopy , plasma protein binding , binding site , structural motif , transcriptional activity , microbiology and biotechnology , biophysics , biology , transcription factor , genetics , biochemistry , virus , gene , stereochemistry
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 hTAF(II)31, whereas the hTAF(II)31-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.