BIOMAT Database Logo BIOMAT Database Logo

Solution structure of the SH3 domain of phospholipase C-gamma. 1993

D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Department of Molecular Physiology, Tokyo Metropolitan Institute of Medical Science, Japan.

SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-gamma (PLC-gamma) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel beta strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of beta structure, the SH3 domain of PLC-gamma is flexible.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
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
D009038 Motion Physical motion, i.e., a change in position of a body or subject as a result of an external force. It is distinguished from MOVEMENT, a process resulting from biological activity. Motions
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010738 Type C Phospholipases A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS. Lecithinase C,Phospholipase C,Phospholipases, Type C,Phospholipases C
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006860 Hydrogen Bonding A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond
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

Related Publications

D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
SH3 in muscles: solution structure of the SH3 domain from nebulin.
February 1998, Journal of molecular biology,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure of N-terminal SH3 domain of Vav and the recognition site for Grb2 C-terminal SH3 domain.
January 2002, Journal of biomolecular NMR,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure of the SH3 domain of DOCK180.
May 2013, Proteins,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
An SH3 domain is required for the mitogenic activity of microinjected phospholipase C-gamma 1.
January 1995, FEBS letters,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II.
July 2006, Biochemistry,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure of the PX domain, a target of the SH3 domain.
June 2001, Nature structural biology,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure of the SH3 domain from Bruton's tyrosine kinase.
March 1998, Biochemistry,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Dynamin binds to SH3 domains of phospholipase C gamma and GRB-2.
June 1994, The Journal of biological chemistry,
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure and peptide binding of the SH3 domain from human Fyn.
June 1996, Structure (London, England : 1993),
D Kohda, and H Hatanaka, and M Odaka, and V Mandiyan, and A Ullrich, and J Schlessinger, and F Inagaki
Solution structure, dynamics, and thermodynamics of the native state ensemble of the Sem-5 C-terminal SH3 domain.
May 2003, Biochemistry,
Copied contents to your clipboard!