Results 211 to 220 of about 24,285 (259)

Atomic structure of the ectodomain from HIV-1 gp41

Nature, 1997
Fusion of viral and cellular membranes by the envelope glycoprotein gp120/gp41 effects entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 and gp41 which remain non-covalently associated. Binding to both CD4 and a co-receptor leads to the conformational changes in gp120/gp41 needed for membrane fusion. We used
W. Weissenhorn, A. Dessen, S. Harrison, J. Skehel, D. C. Wiley   +4 more
semanticscholar   +3 more sources

Two Interaction Modes of the gp41-Derived Peptides With gp41 and Their Correlation With Antimembrane Fusion Activity

Biochemical and Biophysical Research Communications, 1999
Peptides derived from gp41 effectively block the gp41-mediated cell fusion or HIV infection. A 36-mer (naDP178), 51-mer (C51) and 27-mer peptide (C27) from the membrane proximal region of gp41 have been examined their interaction modes with the coiled-coil motif of gp41 presented in thioredoxin (Trx-N) or the bacterially expressed ectodomain of gp41 ...
Moo-Jin Suh, Yeon Gyu Yu, Eun-Rhan Woo
exaly   +3 more sources

HIV-1 gp41 Binding Proteins and Antibodies to gp41 Could Inhibit Enhancement of Human Raji Cell Mhc Class I and II Expression by gp41

Molecular Immunology, 1994
Based on our findings, that HIV-1 soluble gp41 could bind to several proteins on the human, T, B and monocyte cells independently of CD4, we examined the effect of HIV-1 soluble gp41 (sgp41;Env amino acids 539-684) on surface expression of MHC I and II, ICAM-1 and CD21 molecules on human Raji cells.
Hermann Katinger, Ying-Hua Chen, G Böck
exaly   +3 more sources

Three‐Dimensional Solution Structure of the 44 kDa Ectodomain of SIV gp41

EMBO Journal, 1998
The solution structure of the ectodomain of simian immunodeficiency virus (SIV) gp41 (e-gp41), consisting of residues 27–149, has been determined by multi-dimensional heteronuclear NMR spectroscopy.
David G Covell, Michael Caffrey, Paul T. Wingfield   +2 more
exaly   +1 more source

On the Interaction Between gp41 and Membranes: The Immunodominant Loop Stabilizes gp41 Helical Hairpin Conformation

Journal of Molecular Biology, 2003
gp41 is the protein responsible for the process of membrane fusion that allows primate lentiviruses (HIV and SIV) to enter into their host cells. gp41 ectodomain contains an N-terminal and a C-terminal heptad repeat region (NHR and CHR) connected by an immunodominant loop.
Sergio G, Peisajovich, Lior, Blank, Raquel F, Epand, Richard M, Epand, Yechiel, Shai   +4 more
openaire   +2 more sources

Alanine Scanning Mutagenesis of HIV-1 gp41 Heptad Repeat 1: Insight into the gp120−gp41 Interaction

Biochemistry, 2010
On the basis of mutagenesis, biochemical, and structural studies, heptad repeat 1 of HIV gp41 (HR1) has been shown to play numerous critical roles in HIV entry, including interacting with gp120 in prefusion states and interacting with gp41 heptad repeat 2 (HR2) in the fusion state.
Jayita, Sen, Tianran, Yan, Jizhen, Wang, Lijun, Rong, Lin, Tao, Michael, Caffrey   +5 more
openaire   +2 more sources

Antigenic variation of the dominant gp41 epitope in Africa

AIDS, 1993
To determine the value of (combinations of) synthetic peptides representing immunodominant sites on HIV-1/HIV-2 transmembrane proteins for the detection and discrimination between HIV-1 and HIV-2 infection in various populations.Two 24-mer synthetic peptides derived from immunodominant sites on the HIV-1 and HIV-2 transmembrane proteins were used ...
Lange, J. M., Teeuwsen, V. J., Boucher, C. A., Vahlne, A., Barin, F., Tjong-A-Hung, S., Dekker, J., Parkhede, U., de Wolf, F., Goudsmit, J.   +9 more
openaire   +2 more sources

Helical Interactions in the HIV-1 gp41 Core Reveal Structural Basis for the Inhibitory Activity of gp41 Peptides^,

Biochemistry, 2000
The HIV-1 gp41 envelope protein mediates membrane fusion that leads to virus entry into the cell. The core structure of fusion-active gp41 is a six-helix bundle in which an N-terminal three-stranded coiled coil is surrounded by a sheath of antiparallel C-terminal helices.
W, Shu, J, Liu, H, Ji, L, Radigen, S, Jiang, M, Lu   +5 more
openaire   +2 more sources

Time Dependence of Immunoresponse of Different Epitopes of gp41 and Its Relation to the Structure of Short Peptide Fragments of gp41

Collection of Czechoslovak Chemical Communications, 1995
Twenty amino acid residues peptides derived from the N-terminal domain of glycoprotein gp41 exhibit four different types of reactivity with human sera in the course of seroconversion. The differences in the accessibility of the peptide by immune apparatus can result from different binding of the knobs formed by trimers of glycoprotein gp120 to the ...
Dalibor Štys, Ján Novák, Viktor Krchňák, Josef Vágner, Petr Štrop, Miloš Buděšínský   +5 more
openaire   +1 more source

Thermodynamics of Peptide Inhibitor Binding to HIV-1 gp41

Biochemistry, 2001
The gp41 subunit of the human immunodeficiency virus type 1 envelope glycoprotein mediates fusion of the cellular and viral membranes. The gp41 ectodomain is a trimer of alpha-helical hairpins, where N-terminal helices form a parallel three-stranded coiled-coil core and C-terminal helices pack around the core.
J L, Cole, V M, Garsky
openaire   +2 more sources