Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences. 1998

I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
Institute of Biophysics, Biological Research Center, Szeged, Hungary. laczko@everx.szbk.u-szeged.hu

The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, zeta(69-86), zeta(106-126), and zeta(138-155), located in the T cell receptor/CD3 zeta-chain was investigated. Circular dichroism and Fourier-transform infrared spectroscopy of the nonphosphorylated and phosphorylated fragments gave evidence that phosphorylation can alter the secondary structure of the peptides. The most significant--alpha-helix to beta-sheet--conformational change was observed in the case of the zeta(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
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
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
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
D017252 CD3 Complex Complex of at least five membrane-bound polypeptides in mature T-lymphocytes that are non-covalently associated with one another and with the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL). The CD3 complex includes the gamma, delta, epsilon, zeta, and eta chains (subunits). When antigen binds to the T-cell receptor, the CD3 complex transduces the activating signals to the cytoplasm of the T-cell. The CD3 gamma and delta chains (subunits) are separate from and not related to the gamma/delta chains of the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA). Antigens, CD3,CD3 Antigens,T3 Antigens,CD3 Antigen,T3 Antigen,T3 Complex,Antigen, CD3,Antigen, T3,Antigens, T3
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D017550 Spectroscopy, Fourier Transform Infrared A spectroscopic technique in which a range of wavelengths is presented simultaneously with an interferometer and the spectrum is mathematically derived from the pattern thus obtained. FTIR,Fourier Transform Infrared Spectroscopy,Spectroscopy, Infrared, Fourier Transform

Related Publications

I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
November 1988, Journal of immunology (Baltimore, Md. : 1950),
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
January 2003, British journal of haematology,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
January 2006, Advances in medical sciences,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
August 1989, Scandinavian journal of immunology,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
September 1990, Journal of immunology (Baltimore, Md. : 1950),
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
April 2009, Pediatric nephrology (Berlin, Germany),
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
May 1991, Proceedings of the National Academy of Sciences of the United States of America,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
September 2008, European journal of immunology,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
March 2002, Journal of reproductive immunology,
I Laczkó, and M Hollósi, and E Vass, and Z Hegedüs, and E Monostori, and G K Tóth
March 2002, American journal of reproductive immunology (New York, N.Y. : 1989),
Copied contents to your clipboard!