Increasing the Potency and Breadth of an HIV Antibody by Using Structure-Based Rational Design
Copyright policy )Increasing the Potency and Breadth of an HIV Antibody by Using Structure-Based Rational Design
Structural analysis of an HIV antibody reveals residues important for neutralization breadth and potency.
- California Institute of Technology United States
- Howard Hughes Medical Institute United States
- Beth Israel Deaconess Medical Center United States
- Rockefeller University United States
- Charité - University Medicine Berlin Germany
AIDS Vaccines, Binding Sites, Protein Conformation, Molecular Mimicry, Molecular Sequence Data, Antibody Affinity, HIV Antibodies, HIV Envelope Protein gp120, Crystallography, X-Ray, Protein Engineering, Antibodies, Neutralizing, Complementarity Determining Regions, Immunoglobulin Fab Fragments, CD4 Antigens, HIV-1, Humans, Mutant Proteins, Amino Acid Sequence, Immunoglobulin Heavy Chains, Hydrophobic and Hydrophilic Interactions
AIDS Vaccines, Binding Sites, Protein Conformation, Molecular Mimicry, Molecular Sequence Data, Antibody Affinity, HIV Antibodies, HIV Envelope Protein gp120, Crystallography, X-Ray, Protein Engineering, Antibodies, Neutralizing, Complementarity Determining Regions, Immunoglobulin Fab Fragments, CD4 Antigens, HIV-1, Humans, Mutant Proteins, Amino Acid Sequence, Immunoglobulin Heavy Chains, Hydrophobic and Hydrophilic Interactions
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