The association of heavy and light chain variable domains in antibodies: implications for antigen specificity.
KAUST Grant NumberKUK-I1-012-43
Online Publication Date2011-06-28
Print Publication Date2011-08
Permanent link to this recordhttp://hdl.handle.net/10754/596822
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AbstractThe 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.
CitationChailyan A, Marcatili P, Tramontano A (2011) The association of heavy and light chain variable domains in antibodies: implications for antigen specificity. FEBS Journal 278: 2858–2866. Available: http://dx.doi.org/10.1111/j.1742-4658.2011.08207.x.
SponsorsThis 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.
PubMed Central IDPMC3562479
CollectionsPublications Acknowledging KAUST Support
Except where otherwise noted, this item's license is described as Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
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