Morrissey, Kimberly A., Wegrecki, Marcin, Praveena, T., Hansen, Victoria L., Bu, Lijing, Sivaraman, Komagal Kannan, Darko, Samuel, Douek, Daniel C., Rossjohn, Jamie ![]() ![]() |
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Abstract
αβ and γδ T cell receptors (TCRs) are highly diverse antigen receptors that define two evolutionarily conserved T cell lineages. We describe a population of γμTCRs found exclusively in non-eutherian mammals that consist of a two-domain (Vγ-Cγ) γ-chain paired to a three-domain (Vμ-Vμj-Cμ) μ-chain. γμTCRs were characterized by restricted diversity in the Vγ and Vμj domains and a highly diverse unpaired Vμ domain. Crystal structures of two distinct γμTCRs revealed the structural basis of the association of the γμTCR heterodimer. The Vμ domain shared the characteristics of a single-domain antibody within which the hypervariable CDR3μ loop suggests a major antigen recognition determinant. We define here the molecular basis underpinning the assembly of a third TCR lineage, the γμTCR.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Schools > Medicine |
Publisher: | American Association for the Advancement of Science |
ISSN: | 0036-8075 |
Date of First Compliant Deposit: | 14 March 2025 |
Date of Acceptance: | 4 February 2021 |
Last Modified: | 14 Mar 2025 11:15 |
URI: | https://orca.cardiff.ac.uk/id/eprint/176874 |
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