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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
A dimer of the class II αβ heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.
Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.
Comparisons to the soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) protein complex of vesicle fusion suggests that these molecules are all in the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring feature, is involved in the fused mechanism.
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular
Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
The TCP fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and class II MHC molecules, providing evidence that the nature of binding is general.
Structure of influenza haemagglutinin at the pH of membrane fusion
Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes, and reveals a major refolding of the secondary and tertiary structure of the molecule.
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist, providing a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.
Structure of the human class I histocompatibility antigen, HLA-A2
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are
Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified. At least one amino acid substitution in each site seems to be required for the production of
The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign
Atomic structure of the ectodomain from HIV-1 gp41
X-ray crystallography determines the structure of the protease-resistant part of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide, and suggests a common mechanism for initiating fusion.