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À propos de : Crystal Structure of the Broadly Cross-Reactive HIV-1-Neutralizing Fab X5 andFine Mapping of Its Epitope,        

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  • Crystal Structure of the Broadly Cross-Reactive HIV-1-Neutralizing Fab X5 andFine Mapping of Its Epitope,
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  • The human monoclonal antibody Fab X5 neutralizes a broad range of HIV-1 primary isolates.The crystal structure of X5 has been determined at 1.9 Å resolution. There are two crystallographicallyindependent Fab fragments in the asymmetric unit. The crystallographic R value for the final model is0.22. The antibody-combining site features a long (22 amino acid residues) CDR H3 with a protrudinghook-shaped motif. The X5 structure and site-directed mutagenesis data suggest that X5 amino acid residuesW100 and Y100F in the CDR H3 motif may be critical for the binding of Fab X5 to gp120. X5 boundto a complex of a CD4 mimetic and gp120 with approximately the same kinetics and affinity as to aCD4−gp120 complex, suggesting that specific interactions between CD4 and X5 are unlikely to contributeto the binding of X5 to gp120−CD4 complexes. Binding of X5 to alanine scanning mutants of gp120JR-CSF complexed with CD4 suggested a critical role of the highly conserved amino acid residues at positions423 and 432. The X5 structure and fine mapping of its epitope may assist in the elucidation of themechanisms of viral entry and neutralization, and the development of HIV-1 inhibitors and vaccines.
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