 Predicting the Size of the T-Cell Receptor and Antibody Combining Region from Consideration of Efficient Self-Nonself DiscriminationJerome K. Percus, Ora E. Percus and Alan S. Perelson Working Papers from Santa Fe Institute Abstract: The binding of antibody to antigen or T-Cell receptor to major histocompatibility complex-peptide complex requires that portions of the two structures have complementary shapes that can closely approach each other. The question that we address here is how large should the complementary regions on the two sturcutures be. The interacting regions are by necessity roughly the same size. To estimate the size (number of contact residues) of an optimal receptor combining region, we assume that the immune system over evolutionary time has been presented with a large random set of foreign molecules that occur on common pathogens, which it must recognize, and smaller randon set of self-antigens to which it must fail to respond. Evolutionarily, the receptors and the molecular groups that the immune system recognizes as epitoes are imagined to have coevolved to maximize the probability that this task is performed. The probability of a receptor matching a random antigen is estimated from this condition. Using a simple model for receptor-ligand interaction, we estimate that the optimal size binding region on immunoglobulin or T-Cell receptors will contain about 15 contact residues, in agreement with experimental observation. Date: 1993-04 There are no downloads for this item, see the EconPapers FAQ for hints about obtaining it. Related works: Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text Persistent link: https://EconPapers.repec.org/RePEc:wop:safiwp:93-04-019 Access Statistics for this paper More papers in Working Papers from Santa Fe Institute Contact information at EDIRC. |
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