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Article

Mutational analysis of the carboxyl-terminal region of the SV40 major capsid protein VP1.

Journal of biochemistry - 1 Feb 2007

Yokoyama Naoki, Kawano Masa-aki, Tsukamoto Hiroko, Enomoto Teruya, Inoue Takamasa, Takahashi Ryou-u, Nakanishi Akira, Imai Takeshi, Wada Tadashi, Handa Hiroshi

Abstract excerpt

Virus-like particles (VLPs), a promising next-generation drug delivery vehicle, can be formed in vitro using a recombinant viral capsid protein VP1 from SV40. Seventy-two VP1 pentamers interconnect to form the T = 7d lattice of SV40 capsids, through three types of C-terminal interactions, alpha-alpha'-alpha'', beta-beta' and gamma-gamma. These appear to require VP1 conformational switch, which involve in...

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PMID: 17283011
DOI: 10.1093/jb/mvm038

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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