Structural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein

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Title
Structural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein
Author(s)
Chewook Lee; Do-Hyoung Kim; Si-Hyung Lee; J Su; Kyou Hoon Han
Bibliographic Citation
BMB Reports, vol. 49, no. 8, pp. 431-436
Publication Year
2016
Abstract
Human papillomavirus (HPV) is the major cause of cervical cancer, a deadly threat to millions of females. The early oncogene product (E7) of the high-risk HPV16 is the primary agent associated with HPV-related cervical cancers. In order to understand how E7 contributes to the transforming activity, we investigated the structural features of the flexible N-terminal region (46 residues) of E7 by carrying out N-15 heteronuclear NMR experiments and replica exchange molecular dynamics simulations. Several NMR parameters as well as simulation ensemble structures indicate that this intrinsically disordered region of E7 contains two transient (10-20% populated) helical pre-structured motifs that overlap with important target binding moieties such as an E2F-mimic motif and a pRb-binding LXCXE segment. Presence of such target-binding motifs in HPV16 E7 provides a reasonable explanation for its promiscuous target-binding behavior associated with its transforming activity.
Keyword
E7 oncoproteinHuman papillomavirus (HPV)Intrinsically disordered protein (IDP)Molecular dynamics (MD) simulationNuclear magnetic resonance (NMR)Pre-structured motif (PreSMo)
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5483/BMBRep.2016.49.8.021
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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