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Volumn 55, Issue 6, 2000, Pages 455-465

Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin

Author keywords

G protein receptor; Membrane protein; NMR; Peptide; Rhodopsin

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; RHODOPSIN;

EID: 0034080488     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2000.00707.x     Document Type: Article
Times cited : (38)

References (31)
  • 1
    • 0025345316 scopus 로고
    • The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution
    • 1. Weiss, M.S., Wacker, T., Weckesser, J., Welte, W. & Schulz, G.E. (1990) The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution. Febs Lett 267, 268-272.
    • (1990) Febs Lett , vol.267 , pp. 268-272
    • Weiss, M.S.1    Wacker, T.2    Weckesser, J.3    Welte, W.4    Schulz, G.E.5
  • 2
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex: Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetics reaction center from Rhodopseudomonas vindis
    • 2. Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1984) X-ray structure analysis of a membrane protein complex: electron density map at 3 Å resolution and a model of the chromophores of the photosynthetics reaction center from Rhodopseudomonas vindis. J. Mol. Biol. 180, 385-398.
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 3
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: Cofactors and protein-cofactor interactions
    • 3. Ermler, U., Fritzsch, G., Buchanan, S.K. & Michel, H. (1994) Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. Structure 2, 925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 4
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • 4. Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 5
    • 0029652024 scopus 로고
    • Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A
    • 5. Tsukihara, T., Aoyama, H., Yamashita, E., et al. (1995) Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A. Science 269, 1069-1074.
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3
  • 6
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • 6. Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P. & Landau, E.M. (1997) X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 7
    • 0031877366 scopus 로고    scopus 로고
    • Alpha-Hemolysin from Staphylococcus aurens: An archetype of beta-barrel, channel-forming toxins
    • 7. Gouaux, E. (1998) Alpha-Hemolysin from Staphylococcus aurens: an archetype of beta-barrel, channel-forming toxins. J. Struct. Biol. 12, 110-112.
    • (1998) J. Struct. Biol. , vol.12 , pp. 110-112
    • Gouaux, E.1
  • 8
    • 0032478818 scopus 로고    scopus 로고
    • The structure of the potassium channel: Molecular basis of K+ conduction and selectivity
    • 8. Doyle, D.A., Cabral, J.M., Pfuetzner, et al. (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280, 69-77.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1    Cabral, J.M.2
  • 9
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • 9. Schertler, G.R.X., Villa, C. & Henderson, R. (1993) Projection structure of rhodopsin. Nature 362, 770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.R.X.1    Villa, C.2    Henderson, R.3
  • 11
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins
    • 11. Dyson, H.J., Merutka, G., Waltho, J.P., Lerner, R.A. & Wright, P.E. (1992) Folding of peptide fragments comprising the complete sequence of proteins. J. Mol. Biol. 226, 795-817
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 14
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • 14. Yeagle, P.L., Alderfer, J.L. & Albert, A.D. (1995) Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry 34, 14621-14623.
    • (1995) Biochemistry , vol.34 , pp. 14621-14623
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 15
    • 0029391341 scopus 로고
    • Structure of the carboxyl terminal domain of bovine rhodopsin
    • 15. Yeagle, P.L., Alderfer, J.L. & Albert, A.D. (1995) Structure of the carboxyl terminal domain of bovine rhodopsin. Nature Struct. Biol. 2, 832-834.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 832-834
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 16
    • 0030606345 scopus 로고    scopus 로고
    • Structure determination of the fourth cytoplasmic loop and carhoxyl terminal domain of bovine rhodopsin
    • 16. Yeagle, P.L., Alderfer, J.L. & Albert, A.D. (1996) Structure determination of the fourth cytoplasmic loop and carhoxyl terminal domain of bovine rhodopsin. Molecular Vision 2, http://www.molvis.org/molvis/v2/p12/.
    • (1996) Molecular Vision , vol.2
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 17
    • 0030596522 scopus 로고    scopus 로고
    • Free energy determinants of secondary structure formation: β turns and their role in protein folding
    • 17. Yang, A.-S., Hitz, B. & Honig, B. (1996) Free energy determinants of secondary structure formation: β turns and their role in protein folding. J. Mol. Biol. 259, 873-882.
    • (1996) J. Mol. Biol. , vol.259 , pp. 873-882
    • Yang, A.-S.1    Hitz, B.2    Honig, B.3
  • 18
    • 0030841110 scopus 로고    scopus 로고
    • Three dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin
    • 18. Yeagle, P.L., Alderfer, J.L. & Albert, A.D. (1997) Three dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin. Biochemistry 36, 9649-9654.
    • (1997) Biochemistry , vol.36 , pp. 9649-9654
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 20
    • 0019327003 scopus 로고
    • A two-dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • 20. Kumar, A., Ernst, R.R. & Wuthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 21
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton proton distance constraints with nuclear magnetic resonance
    • 21. Wüthrich, K., Billeter, M. & Braun, W.J. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.J.3
  • 22
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS, and GLOMSA
    • 22. Guntert, P., Braunk, W. & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS, and GLOMSA. Mol. Biol. 217, 517-530.
    • (1991) Mol. Biol. , vol.217 , pp. 517-530
    • Guntert, P.1    Braunk, W.2    Wüthrich, K.3
  • 23
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined hy electron cryo-microscopy
    • 23. Unger, V.M. & Schertler, G.F.X. (1995) Low resolution structure of bovine rhodopsin determined hy electron cryo-microscopy. Biophys. J. 68, 1776-1786.
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.X.2
  • 24
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • 24. Grigorieff, N., Ceska, T.A., Downing, K.H., Baldwin, T.M. & Henderson, R. (1996) Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 25
    • 0033982348 scopus 로고    scopus 로고
    • Solution structure of the sixth transmembrane helix of the G-protein coupled receptor, rhodopsin
    • 25. Chopra, A., Yeagle, P.L., Alderfer, J.A. & Albert, A.D. (2000) Solution structure of the sixth transmembrane helix of the G-protein coupled receptor, rhodopsin. Biochim. Biophys. Acta 1463, 217-224.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 217-224
    • Chopra, A.1    Yeagle, P.L.2    Alderfer, J.A.3    Albert, A.D.4
  • 27
    • 0030964858 scopus 로고    scopus 로고
    • The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form β-turns
    • 27. Yeagle, P.L., Alderfer, J.L. & Albert, A.D. (1997) The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form β-turns. Biochemistry 36, 3864-3869.
    • (1997) Biochemistry , vol.36 , pp. 3864-3869
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 28
    • 0030880591 scopus 로고    scopus 로고
    • Solution structure of alpha t alpha, a helical hairpin peptide of de novo design
    • 28. Fezoui, Y., Connolly, P. & Osterhout, J. (1997) Solution structure of alpha t alpha, a helical hairpin peptide of de novo design. Protein Sci. 6, 1869-1877.
    • (1997) Protein Sci. , vol.6 , pp. 1869-1877
    • Fezoui, Y.1    Connolly, P.2    Osterhout, J.3
  • 29
    • 4243229270 scopus 로고    scopus 로고
    • Folding dynamics of a β-hairpin studies by laser temperature jump and kinetic modeling
    • 29. Munoz, V., Thompson, P.A., Henry, E.R., Hofrichter, J. & Eaton, W.A. (1998) Folding dynamics of a β-hairpin studies by laser temperature jump and kinetic modeling. Biophys. J. 74, A175.
    • (1998) Biophys. J. , vol.74
    • Munoz, V.1    Thompson, P.A.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 30
    • 0028068045 scopus 로고
    • Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor
    • 30. Yao, J., Dyson, H.J. & Wright, P.E. (1994) Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor. J. Mol Biol. 243, 736-753.
    • (1994) J. Mol Biol. , vol.243 , pp. 736-753
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 31
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • 31. Baldwin, J.M., Schertler, G.F.X. & Unger, V.M. (1997) An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol 272, 144-164.
    • (1997) J. Mol. Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.X.2    Unger, V.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.