Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region. Export

@article{citeulike:2795364, abstract = {G protein-coupled receptors (GPCRs) play a key step in cellular signal transduction cascades by transducing various extracellular signals via G-proteins. Rhodopsin is a prototypical GPCR involved in the retinal visual signaling cascade. We determined the structure of squid rhodopsin at 3.7 A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade. The structure showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopsin, coupling to G(t), and human beta(2)-adrenergic receptor, coupling to G(s). Notably, squid rhodopsin contains a well-structured cytoplasmic region involved in the interaction with G-proteins, and this region is flexible or disordered in bovine rhodopsin and human beta(2)-adrenergic receptor. The transmembrane helices 5 and 6 are longer and extrude into the cytoplasm. The distal C-terminal tail contains a short hydrophilic alpha-helix CH after the palmitoylated cysteine residues. The residues in the distal C-terminal tail interact with the neighboring residues in the second cytoplasmic loop, the extruded transmembrane helices 5 and 6, and the short helix H8. Additionally, the Tyr111, Asn87, and Asn185 residues are located within hydrogen bonding distances from the nitrogen atom of the Schiff base.}, address = {Structural Biophysics Laboratory, RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148.}, author = {Shimamura, Tatsuro and Hiraki, Kenji and Takahashi, Naoko and Hori, Tetsuya and Ago, Hideo and Masuda, Katsuyoshi and Takio, Koji and Ishiguro, Masaji and Miyano, Masashi}, citeulike-article-id = {2795364}, citeulike-linkout-0 = {http://dx.doi.org/10.1074/jbc.C800040200}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18463093}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18463093}, day = {6}, doi = {10.1074/jbc.C800040200}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {crystallography, cterm, gpcr, rhodopsin, structure, xray}, month = {May}, posted-at = {2008-05-13 16:19:24}, priority = {2}, title = {Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region.}, url = {http://dx.doi.org/10.1074/jbc.C800040200}, year = {2008} }

TY - JOUR ID - citeulike:2795364 L3 - citeulike-article-id:2795364 N2 - G protein-coupled receptors (GPCRs) play a key step in cellular signal transduction cascades by transducing various extracellular signals via G-proteins. Rhodopsin is a prototypical GPCR involved in the retinal visual signaling cascade. We determined the structure of squid rhodopsin at 3.7 A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade. The structure showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopsin, coupling to G(t), and human beta(2)-adrenergic receptor, coupling to G(s). Notably, squid rhodopsin contains a well-structured cytoplasmic region involved in the interaction with G-proteins, and this region is flexible or disordered in bovine rhodopsin and human beta(2)-adrenergic receptor. The transmembrane helices 5 and 6 are longer and extrude into the cytoplasm. The distal C-terminal tail contains a short hydrophilic alpha-helix CH after the palmitoylated cysteine residues. The residues in the distal C-terminal tail interact with the neighboring residues in the second cytoplasmic loop, the extruded transmembrane helices 5 and 6, and the short helix H8. Additionally, the Tyr111, Asn87, and Asn185 residues are located within hydrogen bonding distances from the nitrogen atom of the Schiff base. JF - The Journal of biological chemistry SN - 0021-9258 AD - Structural Biophysics Laboratory, RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148. TI - Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region. KW - crystallography KW - cterm KW - gpcr KW - rhodopsin KW - structure KW - xray AU - Shimamura, Tatsuro AU - Hiraki, Kenji AU - Takahashi, Naoko AU - Hori, Tetsuya AU - Ago, Hideo AU - Masuda, Katsuyoshi AU - Takio, Koji AU - Ishiguro, Masaji AU - Miyano, Masashi PY - 2008/05/06/ UR - http://dx.doi.org/10.1074/jbc.C800040200 ER -