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Structural investigation on the intrinsically disordered N-terminal region of HPV16 E7 protein
- Source :
- BMB Reports
- Publication Year :
- 2016
- Publisher :
- Korean Society for Biochemistry and Molecular Biology - BMB Reports, 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. [BMB Reports 2016; 49(8): 431-436].
- Subjects :
- Human papillomavirus (HPV)
0301 basic medicine
030102 biochemistry & molecular biology
Molecular dynamics (MD) simulation
Chemistry
Stereochemistry
E7 oncoprotein
Pre-structured motif (PreSMo)
General Medicine
Biochemistry
Virology
03 medical and health sciences
Molecular dynamics
030104 developmental biology
Hpv16 e7
Protein structure
Heteronuclear molecule
Intrinsically disordered protein (IDP)
Human papillomavirus
Nuclear magnetic resonance (NMR)
Molecular Biology
Peptide sequence
Target binding
Research Articles
Subjects
Details
- ISSN :
- 19766696
- Volume :
- 49
- Database :
- OpenAIRE
- Journal :
- BMB Reports
- Accession number :
- edsair.doi.dedup.....7ec62f840efe854928e02268caf2bc75