| Literature DB >> 8497064 |
E Decroly1, B Cornet, I Martin, J M Ruysschaert, M Vandenbranden.
Abstract
The secondary structure of the precursor (gp160) of the envelope protein of human immunodeficiency virus type 1 (BH10) and its receptor-binding subunit (gp120) was studied by Fourier-transformed attenuated total reflection spectroscopy. A higher alpha-helix/beta-sheet ratio in the gp120 subunit than in the precursor indicates a structural heterogeneity between the two subunits (gp120 and gp41), in agreement with classical secondary-structure predictions. The secondary structure of gp41 was estimated and compared with existing models. The high alpha-helical content in gp41 and the dominant beta-sheet content in gp120 resemble the distribution in influenza virus hemagglutinin subunits.Entities:
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Year: 1993 PMID: 8497064 PMCID: PMC237702 DOI: 10.1128/JVI.67.6.3552-3560.1993
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103