Organization and orientation of a human T cell receptor δ chain V gene segment that suggests an inversion mechanism is utilized in its rearrangement
- 1 March 1989
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 19 (3) , 571-574
- https://doi.org/10.1002/eji.1830190327
Abstract
A human T cell receptor (TcR) δ chain variable region segment, Vδ3, has been mapped 2 kilobases 3′ to the constant (Cδ) gene. The Vδ3 gene segment is in an inverted transcriptional orientation to the diversity regions (Dδ), joining regions (Jδ) and Cδ gene segments. Analyses of TcR δ cDNA clone, KT041, showed that Vδ3 is linked to Dδ1, Dδ2, Jδ3 and Cδ and that this message encodes a potentially functional TcR δ chain. These findings indicate that a functional TcR δ gene can be constructed through a chromosomal inversion, suggesting that in human, chromosomal inversion is one of the important rearrangement mechanisms.This publication has 38 references indexed in Scilit:
- A new T-cell receptor gene located within the alpha locus and expressed early in T-cell differentiationNature, 1987
- Genomic organization of the genes encoding mouse T-cell receptor α-chainNature, 1985
- Analysis of cDNA clones specific for human T cells and the alpha and beta chains of the T-cell receptor heterodimer from a human T-cell line.Proceedings of the National Academy of Sciences, 1985
- Primary structure of human T-cell receptor α-chainNature, 1984
- A third type of murine T-cell receptor geneNature, 1984
- Genomic organization and sequence of T-cell receptor β-chain constant- and joining-region genesNature, 1984
- Mouse T cell antigen receptor: Structure and organization of constant and joining gene segments encoding the β polypeptideCell, 1984
- Complete primary structure of a heterodimeric T-cell receptor deduced from cDNA sequencesNature, 1984
- Isolation of cDNA clones encoding T cell-specific membrane-associated proteinsNature, 1984
- A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chainsNature, 1984