FEATURES

DESCRIPTION

Also known as TRBR1_HUMAN, TRB. The beta chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA-A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TCR clonotype, it is preferentially selected in effector memory CD8-positive T cells among multiple HLA-A*02:01 carriers/individuals and confers long-lived immunity against IAV infection. Can cross-recognize sporadically emerging IAV variants by molecular mimicry, inducing immunity toward different influenza strains (PubMed:1833769, PubMed:7807026, PubMed:29997621, PubMed:27036003, PubMed:12796775, PubMed:18275829). Antigen recognition initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell differentiation into effector/memory T cells (By similarity). Disulfide-linked heterodimer with TRAV27*01J42*01C*01 alpha chain. The TR primarily interacts via its CDR3-beta domain with M/matrix protein 1-derived peptide (GILGFVFTL) displayed by HLA-A*02.01 in a 'peg-notch' recognition mode (PubMed:27036003, PubMed:12796775, PubMed:18275829). The alpha-beta TR associates with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in the endoplasmic reticulum where a single alpha-beta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 homodimer forming a stable octomeric structure. CD3D-CD3E and CD3G-CD3E heterodimers preferentially associate with TR alpha and TR beta chains (via TM domain), respectively. The association of the CD247 homodimer is the last step of TCR assembly in the endoplasmic reticulum and is required for transport to the cell surface (By similarity).

EXTERNAL LINKS

TRB

Mutations

Mutation(s) distribution

Mutations table