Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism

The murine equivalent of the cDNA encoding the human T11 (CD2) sheep erythrocyte‐binding protein has been cloned. It codes for a putative transmembrane protein which is homologous to human T11. In contrast to immunoglobulins whose domains consist of anti‐parallel β sheets, we predict that mouse and human T11 external domains probably belong to the α/β protein folding class. The cytoplasmic region of T11 is a lengthy, proline‐rich semgent; secondary structural analysis predicts it to have a nonglobular conformation. This elongated tail could allow for interaction with multiple other intracellular proteins and may contain a cation‐binding site involved in T lineage activation.

[1]  E. Reinherz,et al.  Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[2]  Michael Loran Dustin,et al.  Rosetting of activated human T lymphocytes with autologous erythrocytes. Definition of the receptor and ligand molecules as CD2 and lymphocyte function-associated antigen 3 (LFA-3) , 1987, The Journal of experimental medicine.

[3]  E. Reinherz,et al.  Functional and Molecular Aspects of Human T Lymphocyte Activation via T3‐Ti and Tl1 Pathways , 1987 .

[4]  D. Paterson,et al.  Similarities in sequences and cellular expression between rat CD2 and CD4 antigens , 1987, The Journal of experimental medicine.

[5]  B. Haynes,et al.  Thymocyte binding to human thymic epithelial cells is inhibited by monoclonal antibodies to CD-2 and LFA-3 antigens. , 1987, Journal of immunology.

[6]  M. Crumpton,et al.  Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[7]  J. Berg,et al.  Potential metal-binding domains in nucleic acid binding proteins. , 1986, Science.

[8]  S. Tonegawa,et al.  Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[9]  J. C. Pratt,et al.  Activation of cytolytic T lymphocyte and natural killer cell function through the T11 sheep erythrocyte binding protein , 1985, Nature.

[10]  J. Novotný,et al.  Secondary structure of the immunoglobulin J chain. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[11]  G. Reeke,et al.  Three-dimensional structure of beta 2-microglobulin. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[12]  Temple F. Smith,et al.  The statistical distribution of nucleic acid similarities. , 1985, Nucleic acids research.

[13]  E. Reinherz,et al.  Activation of human thymocytes via the 50KD T11 sheep erythrocyte binding protein induces the expression of interleukin 2 receptors on both T3+ and T3- populations. , 1985, Journal of immunology.

[14]  H. Ertl,et al.  Characteristics and functions of Sendai virus-specific T-cell clones , 1984, Journal of virology.

[15]  E. Reinherz,et al.  An alternative pathway of T-cell activation: A functional role for the 50 kd T11 sheep erythrocyte receptor protein , 1984, Cell.

[16]  Charles Auffray,et al.  A program for prediction of protein secondary structure from nucleotide sequence data: application to histocompatibility antigens , 1984, Nucleic Acids Res..

[17]  B. Hoffman,et al.  A simple and very efficient method for generating cDNA libraries. , 1983, Gene.

[18]  H. Okayama,et al.  High-efficiency cloning of full-length cDNA , 1982, Molecular and cellular biology.

[19]  F. Sanger,et al.  DNA sequencing with chain-terminating inhibitors. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[20]  R. M. Burnett,et al.  The structure of the oxidized form of clostridial flavodoxin at 1.9-A resolution. , 1974, The Journal of biological chemistry.

[21]  A. Yonath,et al.  Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline). , 1969, Journal of molecular biology.