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A Model for T Cell Receptor and MHC/Peptide Interaction

Davis, Mark M. and Bjorkman, Pamela J. (1989) A Model for T Cell Receptor and MHC/Peptide Interaction. In: Mechanisms of Lymphocyte Activation and Immune Regulation II. Springer , New York, NY, pp. 13-16. ISBN 978-1-4757-5805-4.

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For some time it has been known that T cell recognition of antigen occurs in an MHC restricted fashion (1–3). Much recent evidence suggests that the antigens ‘seen’ by T cell receptors (TcR) are fragments (presumably derived by intracellular processing) bound to MHC molecules at a single site (4–10) By contrast, the immunoglobulin (Ig) B cell receptor can bind to native antigen alone. Structurally and genetically however, both immunoglobulins and T cell receptors seem very similar. Both are derived from the relatively random juxtaposition of different coding segments (V, D and J) of DNA to produce proteins that differ in their N-terminal domains (V-domains), but are the same elsewhere (C domains) (11–13). Ig V region domains from the heavy and light chain polypeptides (VH and VL) pair to form the ligand binding region (14). By analogy, it seems likely that the binding site for antigen and MHC is formed by pairs of TcR V-domains (either α:β or γ: δ). In the Ig variable regions, sequence diversity is concentrated in three distinct ‘hypervariable regions’(15, 16). These amino acids form the principal points of contact with antigens and are thus referred to as complementarity determining regions (CDR’s) (17, 18).

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Bjorkman, Pamela J.0000-0002-2277-3990
Additional Information:© 1989 Springer Science+Business Media New York.
Record Number:CaltechAUTHORS:20170411-081950060
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:76497
Deposited By: Tony Diaz
Deposited On:11 Apr 2017 16:54
Last Modified:15 Nov 2021 17:00

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