Article
Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody.
Nature structural & molecular biology - 1 Aug 2006
Luftig Micah A, Mattu Marco, Di Giovine Paolo, Geleziunas Romas, Hrin Renee, Barbato Gaetano, Bianchi Elisabetta, Miller Michael D, Pessi Antonello, Carfí Andrea
Abstract excerpt
Elicitation of potent and broadly neutralizing antibodies is an important goal in designing an effective human immunodeficiency virus-1 (HIV-1) vaccine. The HIV-1 gp41 inner-core trimer represents a functionally and structurally conserved target for therapeutics. Here we report the 2.0-A-resolution crystal structure of the complex between the antigen-binding fragment of D5, an HIV-1 cross-neutralizing antibody,...
Topics
- Antibodies, Monoclonal
- Cells, Cultured
- Crystallography, X-Ray
- HIV Envelope Protein gp41
- HIV-1
- Humans
- Hydrophobic and Hydrophilic Interactions
- Leucine
- Models, Molecular
- Mutation
- Neutralization Tests
- Protein Conformation
- Recombinant Fusion Proteins