机构：[1]State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun, 130012, China.[2]Molecular and Computational Biology/Chemistry/Norris Cancer Center, University of Southern California, Los Angeles, CA 90089, USA.[3]Sichuan Tumor Hospital & Institute, Chengdu, 610041, China四川省肿瘤医院[4]The State Engineering Laboratory of AIDS Vaccine, Jilin University, No. 2699, Qianjin Street, Changchun, 130012, China[5]Beijing Health Guard Inc, Beijing, 100176, China
The mono-site mutations of the absolutely conserved residues, (464)LGR(466), in the alpha-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.
基金：
Natural Science Foundation of ChinaNational Natural Science Foundation of China [91027027, 20934002]; State Key Laboratory for Supramolecular Structure and Materials, Jilin UniversityJilin University
第一作者机构：[1]State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun, 130012, China.[2]Molecular and Computational Biology/Chemistry/Norris Cancer Center, University of Southern California, Los Angeles, CA 90089, USA.
通讯作者：
推荐引用方式(GB/T 7714)：
Jin Shi,Pan Dong,Zha Xiao,et al.The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1[J].MOLECULAR BIOSYSTEMS.2014,10(4):724-727.doi:10.1039/c3mb70550a.
APA：
Jin, Shi,Pan, Dong,Zha, Xiao,Yu, Xianghui,Wu, Yuqing...&Chen, Xiaojiang S..(2014).The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1.MOLECULAR BIOSYSTEMS,10,(4)
MLA：
Jin, Shi,et al."The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1".MOLECULAR BIOSYSTEMS 10..4(2014):724-727
