SECONDARY STRUCTURE OF GP160 AND GP120 ENVELOPE GLYCOPROTEINS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 - A FOURIER-TRANSFORM INFRARED SPECTROSCOPIC STUDY

被引:13
|
作者
DECROLY, E [1 ]
CORNET, B [1 ]
MARTIN, I [1 ]
RUYSSCHAERT, JM [1 ]
VANDENBRANDEN, M [1 ]
机构
[1] UNIV LIBRE BRUXELLES,CHIM PHYS MACROMOLEC INTERFACES LAB,CP2062,B-1050 BRUSSELS,BELGIUM
关键词
D O I
10.1128/JVI.67.6.3552-3560.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页码:3552 / 3560
页数:9
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