| Literature DB >> 25818864 |
Ellis L Reinherz1, Jia-huai Wang2.
Abstract
A 1983 Immunology Today rostrum hypothesized that each T cell has two recognition units: a T cell receptor (<span class="Gene">TCR) complex, which binds antigen associated with a polymorphic region of a MHC molecule (pMHC), and a CD4 or CD8 molecule that binds to a conserved region of that same MHC gene product (class II or I, respectively). Structural biology has since precisely revealed those bidentate pMHC interactions. TCRαβ ligates the membrane-distal antigen-binding MHC platform, whereas CD8 clamps a membrane-proximal MHCI α3 domain loop and CD4 docks to a hydrophobic crevice between MHCII α2 and β2 domains. Here, we review how MHC class-restricted binding impacts signaling and lineage commitment, discussing TCR force-driven conformational transitions that may optimally expose the co-receptor docking site on MHC.Entities:
Keywords: TCR; antigen recognition; co-receptor; mechanobiology
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Year: 2015 PMID: 25818864 PMCID: PMC4420642 DOI: 10.1016/j.it.2015.03.004
Source DB: PubMed Journal: Trends Immunol ISSN: 1471-4906 Impact factor: 16.687