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Volumn 12, Issue 6, 2005, Pages 539-544

Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MONOMER; POTASSIUM CHANNEL; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; UNCLASSIFIED DRUG;

EID: 22444444618     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb938     Document Type: Article
Times cited : (167)

References (43)
  • 1
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill, M. & Copello, J.A. Ryanodine receptor calcium release channels. Physiol. Rev. 82, 893-922 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 2
    • 0142155040 scopus 로고    scopus 로고
    • What we don't know about the structure of ryanodine receptor calcium release channels
    • Dulhunty, A.F. & Pouliquin, P. What we don't know about the structure of ryanodine receptor calcium release channels. Clin. Exp. Pharmacol. Physiol. 30, 713-723 (2003).
    • (2003) Clin. Exp. Pharmacol. Physiol. , vol.30 , pp. 713-723
    • Dulhunty, A.F.1    Pouliquin, P.2
  • 3
    • 0036617107 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of ryanodine receptors
    • Wagenknecht, T. & Samsó, M. Three-dimensional reconstruction of ryanodine receptors. Front. Biosci. 7, d1464-d1474 (2002).
    • (2002) Front. Biosci. , vol.7
    • Wagenknecht, T.1    Samsó, M.2
  • 5
    • 4143110231 scopus 로고    scopus 로고
    • The relative position of RyR feet and DHPR tetrads in skeletal muscle
    • Paolini, C., Protasi, F. & Franzini-Armstrong, C. The relative position of RyR feet and DHPR tetrads in skeletal muscle. J. Mol. Biol. 342, 145-153 (2004).
    • (2004) J. Mol. Biol. , vol.342 , pp. 145-153
    • Paolini, C.1    Protasi, F.2    Franzini-Armstrong, C.3
  • 6
    • 0031464972 scopus 로고    scopus 로고
    • Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor
    • Wagenknecht, T. et al. Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor. J. Biol. Chem. 272, 32463-32471 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 32463-32471
    • Wagenknecht, T.1
  • 7
    • 0037059329 scopus 로고    scopus 로고
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor. J. Biol. Chem. 277, 1349-1353 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1349-1353
    • Samsó, M.1    Wagenknecht, T.2
  • 9
    • 0034737734 scopus 로고    scopus 로고
    • Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy
    • Sharma, M.R., Jeyakumar, L.H., Fleischer, S. & Wagenknecht, T. Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy. J. Biol. Chem. 275, 9485-9491 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 9485-9491
    • Sharma, M.R.1    Jeyakumar, L.H.2    Fleischer, S.3    Wagenknecht, T.4
  • 10
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • Radermacher, M. et al. Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J. Cell Biol. 127, 411-423 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 411-423
    • Radermacher, M.1
  • 12
    • 0024318429 scopus 로고
    • Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
    • Takeshima, H. et al. Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 339, 439-445 (1989).
    • (1989) Nature , vol.339 , pp. 439-445
    • Takeshima, H.1
  • 13
    • 0025071723 scopus 로고
    • 2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum
    • 2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 265, 2244-2256 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 2244-2256
    • Zorzato, F.1
  • 14
    • 0029074413 scopus 로고
    • Lumenal sites and C terminus accessibility of the skeletal muscle calcium release channel (ryanodine receptor)
    • Grunwald, R. & Meissner, G. Lumenal sites and C terminus accessibility of the skeletal muscle calcium release channel (ryanodine receptor). J. Biol. Chem. 270, 11338-11347 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 11338-11347
    • Grunwald, R.1    Meissner, G.2
  • 15
    • 0033616799 scopus 로고    scopus 로고
    • Luminal loop of the ryanodine receptor: A pore-forming segment?
    • Balshaw, D., Gao, L. & Meissner, G. Luminal loop of the ryanodine receptor: a pore-forming segment? Proc. Natl. Acad. Sci. USA 96, 3345-3347 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3345-3347
    • Balshaw, D.1    Gao, L.2    Meissner, G.3
  • 16
    • 0033543667 scopus 로고    scopus 로고
    • Molecular identification of the ryanodine receptor pore-forming segment
    • Zhao, M. et al. Molecular identification of the ryanodine receptor pore-forming segment. J. Biol. Chem. 274, 25971-25974 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25971-25974
    • Zhao, M.1
  • 17
    • 16644368098 scopus 로고    scopus 로고
    • A model of the putative pore region of the cardiac ryanodine receptor channel
    • Welch, W., Rheault, S., West, D.J. & Williams, A.J. A model of the putative pore region of the cardiac ryanodine receptor channel. Biophys. J. 87, 2335-2351 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 2335-2351
    • Welch, W.1    Rheault, S.2    West, D.J.3    Williams, A.J.4
  • 19
    • 0942265533 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor) is crucial for channel activation and gating
    • 2+ release channel (ryanodine receptor) is crucial for channel activation and gating. J. Biol. Chem. 279, 3635-3642 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3635-3642
    • Wang, R.1
  • 20
    • 0034981326 scopus 로고    scopus 로고
    • 2+-release channel tunnel: Structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • 2+-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q. Rev. Biophys. 34, 61-104 (2001).
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 21
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 22
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P.B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 23
    • 0032479177 scopus 로고    scopus 로고
    • Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy: Localization of fMet-tRNAfMet and fitting of L1 protein
    • Malhotra, A. et al. Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy: localization of fMet-tRNAfMet and fitting of L1 protein. J. Mol. Biol. 280, 103-116 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 103-116
    • Malhotra, A.1
  • 24
    • 0033606795 scopus 로고    scopus 로고
    • Three-dimensional location of the imperatoxin A binding site on the ryanodine receptor
    • Samsó, M., Trujillo, R., Gurrola, G.B., Valdivia, H.H. & Wagenknecht, T. Three-dimensional location of the imperatoxin A binding site on the ryanodine receptor. J. Cell Biol. 146, 493-499 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 493-499
    • Samsó, M.1    Trujillo, R.2    Gurrola, G.B.3    Valdivia, H.H.4    Wagenknecht, T.5
  • 25
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: Computational tools for intermediate resolution structure interpretation
    • Jiang, W., Baker, M.L., Ludtke, S.J. & Chiu, W. Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308, 1033-1044 (2001).
    • (2001) J. Mol. Biol. , vol.308 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 26
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi, Y. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 35, 25-80 (1998).
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 27
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • Block, B.A., Imagawa, T., Campbell, K.P. & Franzini-Armstrong, C. Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J. Cell Biol. 107, 2587-2600 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 28
    • 0036841939 scopus 로고    scopus 로고
    • Electron tomography of frozen-hydrated isolated triad junctions
    • Wagenknecht, T., Hsieh, C.E., Rath, B.K., Fleischer, S. & Marko, M. Electron tomography of frozen-hydrated isolated triad junctions. Biophys. J. 83, 2491-2501 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 2491-2501
    • Wagenknecht, T.1    Hsieh, C.E.2    Rath, B.K.3    Fleischer, S.4    Marko, M.5
  • 29
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. J. Biol. Chem. 261, 6300-6306 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 30
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229, 1011-1124 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 1011-1124
    • Unwin, N.1
  • 31
    • 0025922079 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum from skeletal and cardiac muscle: Evidence for a sequential mechanism in ryanodine action
    • 2+ release channel of sarcoplasmic reticulum from skeletal and cardiac muscle: evidence for a sequential mechanism in ryanodine action. Mol. Pharmacol. 39, 679-689 (1991).
    • (1991) Mol. Pharmacol. , vol.39 , pp. 679-689
    • Pessah, I.N.1    Zimanyi, I.2
  • 32
    • 0030938245 scopus 로고    scopus 로고
    • Structural components of ryanodine responsible for modulation of sarcoplasmic reticulum calcium channel function
    • Welch, W. et al. Structural components of ryanodine responsible for modulation of sarcoplasmic reticulum calcium channel function. Biochemistry 36, 2939-2950 (1997).
    • (1997) Biochemistry , vol.36 , pp. 2939-2950
    • Welch, W.1
  • 34
    • 0035956880 scopus 로고    scopus 로고
    • Ryanodine receptor point mutant E4032A reveals an allosteric interaction with ryanodine
    • Fessenden, J.D. et al. Ryanodine receptor point mutant E4032A reveals an allosteric interaction with ryanodine. Proc. Natl. Acad. Sci. USA 98, 2865-2870 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2865-2870
    • Fessenden, J.D.1
  • 35
    • 2942711417 scopus 로고    scopus 로고
    • 2+ channel regulation by interdomain interaction within the ryanodine receptor
    • 2+ channel regulation by interdomain interaction within the ryanodine receptor. Biochem. J. 380, 561-569 (2004).
    • (2004) Biochem. J. , vol.380 , pp. 561-569
    • Kobayashi, S.1    Yamamoto, T.2    Parness, J.3    Ikemoto, N.4
  • 36
    • 0036144728 scopus 로고    scopus 로고
    • 2+ spark frequency in skeletal muscle
    • 2+ spark frequency in skeletal muscle. J. Gen. Physiol. 119, 15-32 (2002).
    • (2002) J. Gen. Physiol. , vol.119 , pp. 15-32
    • Shtifman, A.1
  • 37
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y. et al. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417, 515-522 (2002).
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1
  • 38
    • 0029917136 scopus 로고    scopus 로고
    • Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor
    • Wagenknecht, T. et al. Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor. Biophys. J. 70, 1709-1715 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1709-1715
    • Wagenknecht, T.1
  • 39
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 40
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J.A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 41
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff, N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277, 1033-1046 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 42
    • 0033924317 scopus 로고    scopus 로고
    • Accurate calculation of the density of proteins
    • Quillin, M.L. & Matthews, B.W. Accurate calculation of the density of proteins. Acta Crystallogr. D 56, 791-794 (2000).
    • (2000) Acta Crystallogr. D , vol.56 , pp. 791-794
    • Quillin, M.L.1    Matthews, B.W.2
  • 43
    • 0000577528 scopus 로고    scopus 로고
    • Chimera: An extensive molecular modeling application constructed using standard components
    • Huang, C.C., Couch, G.S., Pettersen, E.F. & Ferrin, T.E. Chimera: an extensive molecular modeling application constructed using standard components. Pac. Symp. Biocomput. 1, 724 (1996).
    • (1996) Pac. Symp. Biocomput. , vol.1 , pp. 724
    • Huang, C.C.1    Couch, G.S.2    Pettersen, E.F.3    Ferrin, T.E.4


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