Title |
Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment
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Published in |
BMC Molecular and Cell Biology, April 2013
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DOI | 10.1186/1471-2091-14-9 |
Pubmed ID | |
Authors |
Alex Stewart, Joseph S Harrison, Lauren K Regula, Jonathan R Lai |
Abstract |
Analysis of factors contributing to high affinity antibody-protein interactions provides insight into natural antibody evolution, and guides the design of antibodies with new or enhanced function. We previously studied the interaction between antibody D5 and its target, a designed protein based on HIV-1 gp41 known as 5-Helix, as a model system [Da Silva, G. F.; Harrison, J. S.; Lai, J. R., Biochemistry, 2010, 49, 5464-5472]. Antibody D5 represents an interesting case study because it is derived from the VH1-69 germline segment; this germline segment is characterized by a hydrophobic second heavy chain complementarity determining region (HCDR2) that constitutes the major functional paratope in D5 and several antibodies derived from the same progenitor. |
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