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Article

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

Molecular bioSystems - 1 Apr 2014

Jin Shi, Pan Dong, Zha Xiao, Yu Xianghui, Wu Yuqing, Liu Yongjiang, Yin Fei, Chen Xiaojiang S

Abstract excerpt

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.

Read the complete abstract on PubMed

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Share to Capsid Proteins
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Share to Human papillomavirus 16

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24469550
DOI: 10.1039/c3mb70550a

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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