Issue 4, 2014
From the journal:

Molecular BioSystems

The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1†

Shi Jin,ab   Dong Pan,a   Xiao Zha,ac   Xianghui Yu,d   Yuqing Wu,*a   Yongjiang Liu,e   Fei Yine  and  Xiaojiang S. Chen*b  

* Corresponding authors

a State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun, China
E-mail: yqwu@jlu.edu.cn

b Molecular and Computational Biology/Chemistry/Norris Cancer Center, University of Southern California, Los Angeles, CA 90089, USA
E-mail: xiaojiac@usc.edu

c Sichuan Tumor Hospital & Institute, Chengdu, China

d The State Engineering Laboratory of AIDS Vaccine, Jilin University, No. 2699, Qianjin Street, Changchun, China

e Beijing Health Guard Inc, Beijing, China

Abstract

The mono-site mutations of the absolutely conserved residues, 464LGR466, in the α-helix 5 (h5) of HPV16 L1 completely disrupted the pentamer formation. The implication of this finding is the potential usage of a h5-like peptide as the reagent to interfere with the pentamer formation and stability as an anti-HPV reagent.

Graphical abstract: The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1

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Article information

DOI
https://doi.org/10.1039/C3MB70550A
Article type
Communication
Submitted
03 Dec 2013
Accepted
16 Jan 2014
First published
16 Jan 2014

Mol. BioSyst., 2014,10, 724-727

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The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1

S. Jin, D. Pan, X. Zha, X. Yu, Y. Wu, Y. Liu, F. Yin and X. S. Chen, Mol. BioSyst., 2014, 10, 724 DOI: 10.1039/C3MB70550A

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