What is it about?
Most people think of the tips of the hypervariable loops in antibodies as the principal determinants of their ability to recognize antigens specifically. This is often true, but it is less often appreciated that the orientation of the two proteins (heavy and light chains) comprising an antibody are especially important in configuring the architecture of the combining site.
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Why is it important?
We show, using complex computational tools, that somatic mutations in the interface of the heavy and light chain are particularly important for driving antibody specificity and breadth, especially in the case of the HIV glycoprotein. The work suggests that there are unrealized opportunities for antibody engineering by regulating the interface of heavy and light chains for optimal configuration of antibody combining sites.
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This page is a summary of: Role of antibody heavy and light chain interface residues in affinity maturation of binding to HIV envelope glycoprotein, Molecular Systems Design & Engineering, January 2019, Royal Society of Chemistry,
DOI: 10.1039/c8me00080h.
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