Contribution of light chain residues to high affinity binding in an HIV-1 antibody explored by combinatorial scanning mutagenesis.

@article{Silva2010ContributionOL,
  title={Contribution of light chain residues to high affinity binding in an HIV-1 antibody explored by combinatorial scanning mutagenesis.},
  author={Gustavo F Da Silva and J. S. Heslop Harrison and Jonathan R. Lai},
  journal={Biochemistry},
  year={2010},
  volume={49 26},
  pages={
          5464-72
        }
}
Detailed analysis of factors governing high affinity antibody-antigen interactions yields important insight into molecular recognition and facilitates the design of functional antibody libraries. Here we describe comprehensive mutagenesis of the light chain complementarity determining regions (CDRs) of HIV-1 antibody D5 (which binds its target, "5-Helix", with a reported K(D) of 50 pM). Combinatorial scanning mutagenesis libraries were prepared in which CDR residues on the D5 light chain were… CONTINUE READING
BETA

Figures, Tables, and Topics from this paper.

References

Publications referenced by this paper.
SHOWING 1-10 OF 39 REFERENCES

Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2006
VIEW 13 EXCERPTS
HIGHLY INFLUENTIAL

Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody

M. A. Luftig, M. Mattu, +7 authors A. Carfi
  • Nat. Struct. Mol. Biol
  • 2006
VIEW 17 EXCERPTS
HIGHLY INFLUENTIAL

Rapid mapping of protein functional epitopes by combinatorial alanine scanning.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2000
VIEW 9 EXCERPTS
HIGHLY INFLUENTIAL

Similar Papers

Loading similar papers…