The critical residues of helix 5 for in vitro pentamer formation and stability of the papillomavirus capsid protein, L1.
The mono-site mutations of the absolutely conserved residues, (464)LGR(466), 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.
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun, 130012, China. yqwu@jlu.edu.cn.
Shi
S
Jin
Dong
D
Pan
Xiao
X
Zha
Xianghui
X
Yu
Yuqing
Y
Wu
Yongjiang
Y
Liu
Fei
F
Yin
Xiaojiang S
XS
Chen
D019943:Amino Acid Substitution; D036022:Capsid Proteins / Q000235:genetics* / Q000648:ultrastructure*; D002942:Circular Dichroism; D052162:Human papillomavirus 16 / Q000235:genetics*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009856:Oncogene Proteins, Viral / Q000235:genetics* / Q000648:ultrastructure*; D053918:Papillomavirus Vaccines; D010455:Peptides; D017433:Protein Structure, Secondary / Q000235:genetics; D011506:Proteins / Q000378:metabolism*; D019065:Virus Assembly / Q000235:genetics
D036022:Capsid Proteins; C082750:H5 protein, synthetic; D009856:Oncogene Proteins, Viral; D053918:Papillomavirus Vaccines; D010455:Peptides; D011506:Proteins; C063317:L1 protein, Human papillomavirus type 16