Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Hisato Jingami"'
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:236-241
Metabotropic glutamate receptors (mGluRs) are involved in the regulation of many physiological and pathological processes in the central nervous system. The extracellular domain (ECD) of mGluR subtype 3 (mGluR3) was produced using the baculovirus exp
Publikováno v:
Biochemical and Biophysical Research Communications. 366:373-378
Lipid-mediated regulatory mechanism of the C-terminal ligand binding to PDZ domains is not fully understood, despite their roles in subcellular organization. Here, we provide structural insights into the phosphatidylinositol 4,5-bisphosphate (PIP 2 )
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:627-630
Glutamate is the major excitatory neurotransmitter and its metabotropic glutamate receptor (mGluR) plays an important role in the central nervous system. The ligand-binding domain (LBD) of mGluR subtype 7 (mGluR7) was produced using the baculovirus e
Autor:
Takanori Muto, Takuji Oyama, Hisato Jingami, Takuma Sugi, Shigetada Nakanishi, Kosuke Morikawa
Publikováno v:
The EMBO Journal. 26:2192-2205
Metabotropic glutamate receptors (mGluRs) function as neuronal G-protein-coupled receptors and this requires efficient membrane targeting through associations with cytoplasmic proteins. However, the molecular mechanism regulating mGluR cell-surface t
Publikováno v:
Nucleic Acids Research
The tails of core histones (H2A, H2B, H3 and H4) are critical for the regulation of chromatin dynamics. Each core histone tail is specifically recognized by various tail binding proteins. Here we screened for budding yeast histone H4-tail binding pro
Negative Cooperativity of Glutamate Binding in the Dimeric Metabotropic Glutamate Receptor Subtype 1
Publikováno v:
Journal of Biological Chemistry. 279:35526-35534
Metabotropic glutamate receptor (mGluR) subtype 1 is a Class III G-protein-coupled receptor that is mainly expressed on the post-synaptic membrane of neuronal cells. The receptor has a large N-terminal extracellular ligand binding domain that forms a
Autor:
Masayuki Hirose, Shigeru Yanagi, Takanori Muto, Yoshiaki Nakajima, Hirohei Yamamura, Koki Moriyoshi, Jun Kitano, Shigetada Nakanishi, Hisato Jingami
Publikováno v:
Journal of Biological Chemistry. 279:32308-32315
Tamalin is a scaffold protein that forms a multiple protein assembly including metabotropic glutamate receptors (mGluRs) and several postsynaptic and protein-trafficking scaffold proteins in distinct mode of protein-protein association. In the presen
Publikováno v:
Journal of Biological Chemistry. 278:11344-11350
In contrast to the classical nuclear receptors, the constitutive androstane receptor (CAR) is transcriptionally active in the absence of ligand. In the course of searching for the mediator of CAR activation, we found that ligand-independent activatio
Publikováno v:
Journal of Biological Chemistry. 278:4314-4321
Previously, we determined the crystal structures of the dimeric ligand binding region of the metabotropic glutamate receptor subtype 1. Each protomer binds l-glutamate within the crevice between the LB1 and LB2 domains. We proposed that the two diffe
Publikováno v:
Proceedings of the National Academy of Sciences. 99:2660-2665
Crystal structures of the extracellular ligand-binding region of the metabotropic glutamate receptor, complexed with an antagonist, (S)-(α)-methyl-4-carboxyphenylglycine, and with both glutamate and Gd 3+ ion, have been determined by x-ray crystallo