Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Jun;83(12):4461–4463. doi: 10.1073/pnas.83.12.4461

Subgroups of variable region genes of beta chains of T-cell receptors for antigen.

M Schiffer, T T Wu, E A Kabat
PMCID: PMC323753  PMID: 3487089

Abstract

The beta-chain variable regions of 6 human, 21 mouse, and 1 rabbit T-cell receptors for antigen, including two pairs of duplicates, have been classified into two subgroups. Subgroup I has an invariant Phe at residue 65 and a salt bridge can be formed between the Asp at position 86 and the 11 Arg, 2 Lys, and 1 His residues at position 64. In one instance Tyr replaces Asp at position 86 so that a salt bridge cannot be formed with the Lys at position 64. Subgroup II has an invariant Tyr at residue 65; 8 chains have Gly and 3 have Ala at position 63. These 3 have Asp at position 64. Those with Gly-63 cannot form a salt bridge in this region of the beta chain. The 3 with Asp-64 have Arg at position 86, can form a reverse salt bridge, and could constitute a third subgroup. The relation of these findings to functional parameters in beta chains of the T-cell receptors for antigen deserves further study. The use of variability plots on the assumption that the beta chains are a single population may be misleading for the variable region. Most of the variability in the expressed beta chains would be created by variable-diversity-joining assortment, junctional diversity, and the possible insertion of N sequences.

Full text

PDF
4463

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barth R. K., Kim B. S., Lan N. C., Hunkapiller T., Sobieck N., Winoto A., Gershenfeld H., Okada C., Hansburg D., Weissman I. L. The murine T-cell receptor uses a limited repertoire of expressed V beta gene segments. Nature. 1985 Aug 8;316(6028):517–523. doi: 10.1038/316517a0. [DOI] [PubMed] [Google Scholar]
  2. Behlke M. A., Spinella D. G., Chou H. S., Sha W., Hartl D. L., Loh D. Y. T-cell receptor beta-chain expression: dependence on relatively few variable region genes. Science. 1985 Aug 9;229(4713):566–570. doi: 10.1126/science.3875151. [DOI] [PubMed] [Google Scholar]
  3. Bernstein F. C., Koetzle T. F., Williams G. J., Meyer E. F., Jr, Brice M. D., Rodgers J. R., Kennard O., Shimanouchi T., Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol. 1977 May 25;112(3):535–542. doi: 10.1016/s0022-2836(77)80200-3. [DOI] [PubMed] [Google Scholar]
  4. Chien Y. H., Gascoigne N. R., Kavaler J., Lee N. E., Davis M. M. Somatic recombination in a murine T-cell receptor gene. Nature. 1984 May 24;309(5966):322–326. doi: 10.1038/309322a0. [DOI] [PubMed] [Google Scholar]
  5. Epp O., Lattman E. E., Schiffer M., Huber R., Palm W. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-A resolution. Biochemistry. 1975 Nov 4;14(22):4943–4952. doi: 10.1021/bi00693a025. [DOI] [PubMed] [Google Scholar]
  6. Furey W., Jr, Wang B. C., Yoo C. S., Sax M. Structure of a novel Bence-Jones protein (Rhe) fragment at 1.6 A resolution. J Mol Biol. 1983 Jul 5;167(3):661–692. doi: 10.1016/s0022-2836(83)80104-1. [DOI] [PubMed] [Google Scholar]
  7. Hedrick S. M., Nielsen E. A., Kavaler J., Cohen D. I., Davis M. M. Sequence relationships between putative T-cell receptor polypeptides and immunoglobulins. Nature. 1984 Mar 8;308(5955):153–158. doi: 10.1038/308153a0. [DOI] [PubMed] [Google Scholar]
  8. Jones N., Leiden J., Dialynas D., Fraser J., Clabby M., Kishimoto T., Strominger J. L., Andrews D., Lane W., Woody J. Partial primary structure of the alpha and beta chains of human tumor T-cell receptors. Science. 1985 Jan 18;227(4684):311–314. doi: 10.1126/science.3871253. [DOI] [PubMed] [Google Scholar]
  9. Kabat E. A., Wu T. T. Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains. Ann N Y Acad Sci. 1971 Dec 31;190:382–393. doi: 10.1111/j.1749-6632.1971.tb13550.x. [DOI] [PubMed] [Google Scholar]
  10. Marquart M., Deisenhofer J., Huber R., Palm W. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.0 A resolution. J Mol Biol. 1980 Aug 25;141(4):369–391. doi: 10.1016/0022-2836(80)90252-1. [DOI] [PubMed] [Google Scholar]
  11. Patten P., Yokota T., Rothbard J., Chien Y., Arai K., Davis M. M. Structure, expression and divergence of T-cell receptor beta-chain variable regions. Nature. 1984 Nov 1;312(5989):40–46. doi: 10.1038/312040a0. [DOI] [PubMed] [Google Scholar]
  12. Saito H., Kranz D. M., Takagaki Y., Hayday A. C., Eisen H. N., Tonegawa S. Complete primary structure of a heterodimeric T-cell receptor deduced from cDNA sequences. 1984 Jun 28-Jul 4Nature. 309(5971):757–762. doi: 10.1038/309757a0. [DOI] [PubMed] [Google Scholar]
  13. Saul F. A., Amzel L. M., Poljak R. J. Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution. J Biol Chem. 1978 Jan 25;253(2):585–597. [PubMed] [Google Scholar]
  14. Segal D. M., Padlan E. A., Cohen G. H., Rudikoff S., Potter M., Davies D. R. The three-dimensional structure of a phosphorylcholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298–4302. doi: 10.1073/pnas.71.11.4298. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Siu G., Clark S. P., Yoshikai Y., Malissen M., Yanagi Y., Strauss E., Mak T. W., Hood L. The human T cell antigen receptor is encoded by variable, diversity, and joining gene segments that rearrange to generate a complete V gene. Cell. 1984 Jun;37(2):393–401. doi: 10.1016/0092-8674(84)90369-6. [DOI] [PubMed] [Google Scholar]
  16. Tunnacliffe A., Kefford R., Milstein C., Forster A., Rabbitts T. H. Sequence and evolution of the human T-cell antigen receptor beta-chain genes. Proc Natl Acad Sci U S A. 1985 Aug;82(15):5068–5072. doi: 10.1073/pnas.82.15.5068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Williams A. F. Immunoglobulin-related domains for cell surface recognition. Nature. 1985 Apr 18;314(6012):579–580. doi: 10.1038/314579a0. [DOI] [PubMed] [Google Scholar]
  18. Wu T. T., Kabat E. A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Yanagi Y., Yoshikai Y., Leggett K., Clark S. P., Aleksander I., Mak T. W. A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains. Nature. 1984 Mar 8;308(5955):145–149. doi: 10.1038/308145a0. [DOI] [PubMed] [Google Scholar]
  20. Yoshikai Y., Anatoniou D., Clark S. P., Yanagi Y., Sangster R., Van den Elsen P., Terhorst C., Mak T. W. Sequence and expression of transcripts of the human T-cell receptor beta-chain genes. Nature. 1984 Dec 6;312(5994):521–524. doi: 10.1038/312521a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES