BIOMAT Database Logo BIOMAT Database Logo

NMR assignment of the phosphotyrosine binding (PTB) domain of tensin. 2006

Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
Burnham Institute for Medical Research, Infectious and Inflammatory Disease Center and Cancer Center, 10901 North Torrey Pines Rd, La Jolla, California 92037, USA.

UI MeSH Term Description Entries
D008840 Microfilament Proteins Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
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
D000070876 Tensins A family of multidomain microfilament proteins that bind ACTIN FILAMENTS and INTEGRINS at FOCAL ADHESIONS. They generally consist of an N-terminal domain with homology to PHOSPHOTYROSINE PHOSPHATASE, a C2 DOMAIN; unique central regions rich in PROLINE; ALANINE; GLYCINE; and SERINE; an SH2 DOMAIN; and a C-terminal phosphotyrosine-binding region. They are involved in CELL MIGRATION; CELL ADHESION; SIGNAL TRANSDUCTION; and reorganization of the CYTOSKELETON. Tensin
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
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D016023 Integrins A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors (RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation. Integrin
D019000 Phosphotyrosine An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis. Tyrosine-O-phosphate,Tyrosine O phosphate
D019906 Nuclear Magnetic Resonance, Biomolecular NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope. Biomolecular Nuclear Magnetic Resonance,Heteronuclear Nuclear Magnetic Resonance,NMR Spectroscopy, Protein,NMR, Biomolecular,NMR, Heteronuclear,NMR, Multinuclear,Nuclear Magnetic Resonance, Heteronuclear,Protein NMR Spectroscopy,Biomolecular NMR,Heteronuclear NMR,Multinuclear NMR,NMR Spectroscopies, Protein,Protein NMR Spectroscopies,Spectroscopies, Protein NMR,Spectroscopy, Protein NMR

Related Publications

Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
Structure and function of the phosphotyrosine binding (PTB) domain.
January 1995, Progress in biophysics and molecular biology,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine.
May 1995, Science (New York, N.Y.),
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
Integrin {beta}3 phosphorylation dictates its complex with the Shc phosphotyrosine-binding (PTB) domain.
November 2010, The Journal of biological chemistry,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
Structural and evolutionary division of phosphotyrosine binding (PTB) domains.
January 2005, Journal of molecular biology,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
Sequential NMR assignment of the RAS-binding domain of Byr2.
April 2000, Journal of biomolecular NMR,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
NMR assignment of the mTOR domain responsible for rapamycin binding.
January 2006, Journal of biomolecular NMR,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
NMR assignment of the Cyclin T-binding domain of human Hexim1.
January 2006, Journal of biomolecular NMR,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
NMR assignment of the C-terminal actin-binding domain of talin.
June 2008, Biomolecular NMR assignments,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
The dynein stalk head, the microtubule binding-domain of dynein: NMR assignment and ligand binding.
June 2008, Journal of biomolecular NMR,
Marilisa Leone, and Eric Chi-Wang Yu, and Robert Liddington, and Maurizio Pellecchia
NMR assignment of the cAMP-binding domain A of the PKA regulatory subunit.
January 2006, Journal of biomolecular NMR,
Copied contents to your clipboard!