Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2858-2866 |
| Number of pages | 9 |
| Journal | FEBS Journal |
| Volume | 278 |
| Issue number | 16 |
| DOIs | |
| State | Published - Jun 28 2011 |
| Externally published | Yes |
Bibliographical note
KAUST Repository Item: Exported on 2020-10-01Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: This work was partially supported by Award No. KUK-I1-012-43 made by the King Abdullah University of Science and Technology (KAUST), by Fondazione Roma and by the Italian Ministry of Health, contract no. onc_ord 25/07, FIRB ITALBIONET and PROTEOMICA.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.