Secondary structure of gp160 and gp120 envelope glycoproteins of human immunodeficiency virus type 1: a Fourier transform infrared spectroscopic study.
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.
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
E
E
Decroly
B
B
Cornet
I
I
Martin
J M
JM
Ruysschaert
M
M
Vandenbranden
D015704:CD4 Antigens / Q000737:chemistry / Q000378:metabolism; D005583:Fourier Analysis; D015686:Gene Products, env / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D019302:HIV Envelope Protein gp160; D015700:HIV Envelope Protein gp41 / Q000737:chemistry; D015497:HIV-1 / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry; D011498:Protein Precursors / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared
D015704:CD4 Antigens; D015686:Gene Products, env; D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D015700:HIV Envelope Protein gp41; D008081:Liposomes; D011498:Protein Precursors