BIOMAT Database Logo BIOMAT Database Logo

Complete primary structure of a heterodimeric T-cell receptor deduced from cDNA sequences. 1984

H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa

Two related, but distinct, cDNA clones have been isolated and sequenced from a functional murine cytotoxic T-lymphocyte clone. The genes corresponding to these cDNA are expressed and rearranged specifically in T cells and both have similarities to immunoglobulin variable and constant region genes. It is concluded that these genes code for the two subunits of the heterodimeric antigen receptor on the surface of the T cell; its complete deduced primary structure is presented.

UI MeSH Term Description Entries
D007127 Immunoglobulin Constant Regions The domains of the immunoglobulin molecules that are invariable in their amino acid sequence within any class or subclass of immunoglobulin. They confer biological as well as structural functions to immunoglobulins. One each on both the light chains and the heavy chains comprises the C-terminus half of the IMMUNOGLOBULIN FAB FRAGMENT and two or three of them make up the rest of the heavy chains (all of the IMMUNOGLOBULIN FC FRAGMENT) Ig Constant Regions,Immunoglobulin Constant Region,Constant Region, Ig,Constant Region, Immunoglobulin,Constant Regions, Ig,Constant Regions, Immunoglobulin,Regions, Ig Constant
D007135 Immunoglobulin Variable Region That region of the immunoglobulin molecule that varies in its amino acid sequence and composition, and comprises the binding site for a specific antigen. It is located at the N-terminus of the Fab fragment of the immunoglobulin. It includes hypervariable regions (COMPLEMENTARITY DETERMINING REGIONS) and framework regions. Variable Region, Ig,Variable Region, Immunoglobulin,Framework Region, Immunoglobulin,Fv Antibody Fragments,Fv Fragments,Ig Framework Region,Ig Variable Region,Immunoglobulin Framework Region,Immunoglobulin Fv Fragments,Immunoglobulin V,Antibody Fragment, Fv,Antibody Fragments, Fv,Fragment, Fv,Fragment, Fv Antibody,Fragment, Immunoglobulin Fv,Fragments, Fv,Fragments, Fv Antibody,Fragments, Immunoglobulin Fv,Framework Region, Ig,Framework Regions, Ig,Framework Regions, Immunoglobulin,Fv Antibody Fragment,Fv Fragment,Fv Fragment, Immunoglobulin,Fv Fragments, Immunoglobulin,Ig Framework Regions,Ig Variable Regions,Immunoglobulin Framework Regions,Immunoglobulin Fv Fragment,Immunoglobulin Variable Regions,Regions, Immunoglobulin Variable,Variable Regions, Ig,Variable Regions, Immunoglobulin
D011948 Receptors, Antigen, T-Cell Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (CD3 COMPLEX). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains. Antigen Receptors, T-Cell,T-Cell Receptors,Receptors, T-Cell Antigen,T-Cell Antigen Receptor,T-Cell Receptor,Antigen Receptor, T-Cell,Antigen Receptors, T Cell,Receptor, T-Cell,Receptor, T-Cell Antigen,Receptors, T Cell Antigen,Receptors, T-Cell,T Cell Antigen Receptor,T Cell Receptor,T Cell Receptors,T-Cell Antigen Receptors
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004262 DNA Restriction Enzymes Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1. Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Complete primary structure of lamb preprochymosin deduced from cDNA.
August 1990, Nucleic acids research,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences.
August 1990, Journal of biochemistry,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Rabbit serum amyloid protein A: expression and primary structure deduced from cDNA sequences.
December 1991, Scandinavian journal of immunology,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Complete primary structures of two major murine serum amyloid A proteins deduced from cDNA sequences.
May 1985, Proceedings of the National Academy of Sciences of the United States of America,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence.
December 1984, Cell,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Primary structure of chicken skeletal muscle and fibroblast alpha-actinins deduced from cDNA sequences.
November 1988, European journal of biochemistry,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences.
October 1989, Journal of biochemistry,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones.
December 1987, The Journal of biological chemistry,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Primary structure of porcine cardiac muscarinic acetylcholine receptor deduced from the cDNA sequence.
December 1986, FEBS letters,
H Saito, and D M Kranz, and Y Takagaki, and A C Hayday, and H N Eisen, and S Tonegawa
Primary structure of the T3 gamma subunit of the T3/T cell antigen receptor complex deduced from cDNA sequences: evolution of the T3 gamma and delta subunits.
August 1986, The EMBO journal,
Copied contents to your clipboard!