Journal
FEBS JOURNAL
Volume 278, Issue 16, Pages 2858-2866Publisher
WILEY
DOI: 10.1111/j.1742-4658.2011.08207.x
Keywords
antigen binding; immunoglobulins; interface; structure analysis; variable domain packing
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Funding
- King Abdullah University of Science and Technology (KAUST) [KUK-I1-012-43]
- Fondazione Roma
- Italian Ministry of Health [onc_ord 25/07]
- FIRB ITALBIONET
- PROTEOMICA
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The antigen-binding site of immunoglobulins is formed by six regions, three from the light and three from the heavy chain variable domains, which, on association of the two chains, form the conventional antigen-binding site of the antibody. The mode of interaction between the heavy and light chain variable domains affects the relative position of the antigen-binding loops and therefore has an effect on the overall conformation of the binding site. In this article, we analyze the structure of the interface between the heavy and light chain variable domains and show that there are essentially two different modes for their interaction that can be identified by the presence of key amino acids in specific positions of the antibody sequences. We also show that the different packing modes are related to the type of recognized antigen.
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