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

被引：15

作者：

Kim, Do-Hyoung ^{[1
]}

Lee, Si-Hyung ^{[1
]}

Nam, Ki Hoon ^{[1
,3
]}

Chi, Seung-Wook ^{[2
]}

Chang, Iksoo ^{[3
]}

Han, Kyou-Hoon ^{[1
]}

机构：

[1] KRIBB, Bioinformat Res Ctr, Taejon 305806, South Korea

[2] KRIBB, Med Prote Res Ctr, Taejon 305806, South Korea

[3] Pusan Natl Univ, Dept Phys, Computat Prote & Biophys Lab, Pusan 609735, South Korea

来源：

BMB REPORTS | 2009年 / 42卷 / 07期

关键词：

Herpes simplex virus; hTAF(II)31; Intrinsically unfolded protein; NMR; Transcriptional activation domain; VP16; HERPES-SIMPLEX-VIRUS; HEPATITIS-B-VIRUS; HETERONUCLEAR NMR-SPECTROSCOPY; TRANSACTIVATION DOMAIN; UNSTRUCTURED PROTEINS; SECONDARY STRUCTURE; BINDING PROTEIN; HUMAN P53; COMPLEX; MECHANISMS;

D O I：

10.5483/BMBRep.2009.42.7.411

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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,131, 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 pre-structured motifs mediate promiscuous binding to various target proteins. [BMB reports 2009; 42(7): 411-417]

引用

页码：411 / 417

页数：7