High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
暂无分享,去创建一个
[1] Duilio Cascio,et al. Structural determinants of nitroxide motion in spin‐labeled proteins: Solvent‐exposed sites in helix B of T4 lysozyme , 2008, Protein science : a publication of the Protein Society.
[2] H. Hamm,et al. Heterotrimeric G protein activation by G-protein-coupled receptors , 2008, Nature Reviews Molecular Cell Biology.
[3] W. Hubbell,et al. Sequence of late molecular events in the activation of rhodopsin , 2007, Proceedings of the National Academy of Sciences.
[4] R. Stevens,et al. High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor , 2007, Science.
[5] R. Stevens,et al. GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function , 2007, Science.
[6] D. Siderovski,et al. Receptor-Mediated Activation of Heterotrimeric G-Proteins: Current Structural Insights , 2007, Molecular Pharmacology.
[7] Martin Heck,et al. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit , 2007, Proceedings of the National Academy of Sciences.
[8] Duilio Cascio,et al. Structural determinants of nitroxide motion in spin‐labeled proteins: Tertiary contact and solvent‐inaccessible sites in helix G of T4 lysozyme , 2007, Protein science : a publication of the Protein Society.
[9] B. Kobilka. G protein coupled receptor structure and activation. , 2007, Biochimica et biophysica acta.
[10] Krzysztof Palczewski,et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin , 2006, Proceedings of the National Academy of Sciences.
[11] C. Altenbach,et al. Conformational states and dynamics of rhodopsin in micelles and bilayers. , 2006, Biochemistry.
[12] Viktor Hornak,et al. Location of Trp265 in metarhodopsin II: implications for the activation mechanism of the visual receptor rhodopsin. , 2006, Journal of molecular biology.
[13] T. Schwartz,et al. Molecular mechanism of 7TM receptor activation--a global toggle switch model. , 2006, Annual review of pharmacology and toxicology.
[14] Marcus Elstner,et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. , 2004, Journal of molecular biology.
[15] Wei Liu,et al. Helix packing moments reveal diversity and conservation in membrane protein structure. , 2004, Journal of molecular biology.
[16] Manfred Burghammer,et al. Structure of bovine rhodopsin in a trigonal crystal form. , 2003, Journal of molecular biology.
[17] D. Cafiso,et al. Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein. , 2003, Biochemistry.
[18] H Gobind Khorana,et al. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. , 2003, Advances in protein chemistry.
[19] J. Ballesteros,et al. Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. , 2002, The Journal of biological chemistry.
[20] Linda Columbus,et al. A new spin on protein dynamics. , 2002, Trends in biochemical sciences.
[21] Yoshinori Shichida,et al. Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[22] K. Palczewski,et al. Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor , 2002, Chembiochem : a European journal of chemical biology.
[23] K. Hideg,et al. Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. , 2001, Biochemistry.
[24] J. Klein-Seetharaman,et al. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. , 2001, Biochemistry.
[25] J. Klein-Seetharaman,et al. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8. , 2001, Biochemistry.
[26] D C Teller,et al. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). , 2001, Biochemistry.
[27] T. Kálai,et al. Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure. , 2001, Biochemistry.
[28] Mark S.P. Sansom,et al. Hinges, swivels and switches: the role of prolines in signalling via transmembrane α-helices , 2000 .
[29] K. J. Oh,et al. Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. , 2000, Biochemistry.
[30] G. Jeschke,et al. Dead-time free measurement of dipole-dipole interactions between electron spins. , 2000, Journal of magnetic resonance.
[31] H. Khorana,et al. Structural features of the C-terminal domain of bovine rhodopsin: a site-directed spin-labeling study. , 1999, Biochemistry.
[32] C Altenbach,et al. Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study. , 1999, Biochemistry.
[33] J. Klein-Seetharaman,et al. Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study. , 1999, Biochemistry.
[34] H. Khorana,et al. Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin , 1996, Science.
[35] O. Lichtarge,et al. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F , 1996, Nature.
[36] H. Khorana,et al. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. , 1996, Biochemistry.
[37] S. W. Lin,et al. Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. , 1996, Biochemistry.
[38] K. Hideg,et al. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. , 1996, Biochemistry.
[39] Y. Shin,et al. Determination of the distance between two spin labels attached to a macromolecule. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[40] H. Khorana,et al. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. , 1995, Biochemistry.
[41] H. Weinstein,et al. Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor. , 1994, Protein engineering.
[42] H. Khorana,et al. Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. , 1993, Biochemistry.
[43] K. Hofmann,et al. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[44] H. Khorana,et al. Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. , 1987, Proceedings of the National Academy of Sciences of the United States of America.