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Volumn 468, Issue 7323, 2010, Pages 585-588

The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2;

EID: 78649469923     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09471     Document Type: Article
Times cited : (168)

References (37)
  • 1
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • Giannini, G., Conti, A., Mammarella, S., Scrobogna, M. &Sorrentino, V. The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues. J. Cell Biol. 128,893-904(1995).
    • (1995) J. Cell Biol. , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 2
    • 77955562391 scopus 로고    scopus 로고
    • Ryanodine receptor channelopathies
    • Betzenhauser, M. J. & Marks, A. R. Ryanodine receptor channelopathies. Pflugers Arch. 460,467-480 (2010).
    • (2010) Pflugers Arch. , vol.460 , pp. 467-480
    • Betzenhauser, M.J.1    Marks, A.R.2
  • 3
    • 33748997392 scopus 로고    scopus 로고
    • Mutations in RYR1 in malignant hyperthermia and central core disease
    • Robinson, R., Carpenter, D., Shaw, M.A., Halsall, J.& Hopkins, P. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum. Mutat 27,977-989 (2006).
    • (2006) Hum. Mutat , vol.27 , pp. 977-989
    • Robinson, R.1    Carpenter, D.2    Shaw, M.A.3    Halsall, J.4    Hopkins, P.5
  • 5
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembranedomainsoftheRyR1calciumrelease channelbycryo-EM
    • Samsó, M., Wagenknecht, T. & Allen, P. D. Internal structure and visualization of transmembranedomainsoftheRyR1calciumrelease channelbycryo-EM. Nature Struct. Mol. Biol. 12, 539-544 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 539-544
    • Samsó, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 6
    • 67650388595 scopus 로고    scopus 로고
    • 21releaseasatriggering mechanism for CPVT and MH episodes caused by mutations in RYR and CASQ genes
    • 21releaseasatriggering mechanism for CPVT and MH episodes caused by mutations in RYR and CASQ genes. J. Physiol. (Lond.) 587, 3113-3115 (2009).
    • (2009) J. Physiol. (Lond.) , vol.587 , pp. 3113-3115
    • MacLennan, D.H.1    Chen, S.R.2
  • 7
    • 67650469595 scopus 로고    scopus 로고
    • Crystal structure of type i ryanodine receptor amino-terminal b-trefoil domain reveals a disease-associated mutation 'hot spot' loop
    • Amador, F. J. et al. Crystal structure of type I ryanodine receptor amino-terminal b-trefoil domain reveals a disease-associated mutation 'hot spot' loop. Proc. Natl Acad. Sci. USA 106, 11040-11044 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11040-11044
    • Amador, F.J.1
  • 8
    • 70350709897 scopus 로고    scopus 로고
    • Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: Insights into disease mutations
    • Lobo, P. A. & Van Petegem, F. Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations. Structure 17, 1505-1514 (2009).
    • (2009) Structure , vol.17 , pp. 1505-1514
    • Lobo, P.A.1    Van Petegem, F.2
  • 9
    • 67649637588 scopus 로고    scopus 로고
    • Coordinatedmovementofcytoplasmic and transmembrane domains of RyR1 upon gating
    • Samsó,M.,Feng,W.,Pessah,I.N.&Allen,P.D. Coordinatedmovementofcytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol. 7, e85 (2009).
    • (2009) PLoS Biol. , vol.7
    • Samsó, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 10
    • 33847266703 scopus 로고    scopus 로고
    • ADP-EM: Fast exhaustive multi-resolutiondockingforhigh-throughputcoverage
    • Garzon, J. I., Kovacs, J., Abagyan, R. & Chacon, P. ADP-EM: fast exhaustive multi-resolutiondockingforhigh-throughputcoverage.Bioinformatics23, 427-433(2007).
    • (2007) Bioinformatics , vol.23 , pp. 427-433
    • Garzon, J.I.1    Kovacs, J.2    Abagyan, R.3    Chacon, P.4
  • 11
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacón, P. & Wriggers, W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317, 375-384 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacón, P.1    Wriggers, W.2
  • 13
    • 0035932955 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localizationof its amino terminus
    • Liu, Z. et al. Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localizationof its amino terminus. Proc. Natl Acad. Sci. USA 98, 6104-6109 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6104-6109
    • Liu, Z.1
  • 14
    • 34547104383 scopus 로고    scopus 로고
    • 2-terminal disease-causing mutation hot spot to the 'clamp' region in the three-dimensional structure of the cardiac ryanodine receptor
    • 2-terminal disease-causing mutation hot spot to the 'clamp' region in the three-dimensional structure of the cardiac ryanodine receptor. J. Biol. Chem. 282, 17785-17793 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 17785-17793
    • Wang, R.1
  • 15
    • 0037125792 scopus 로고    scopus 로고
    • 21releasechannelhasanoxidoreductase-like domain
    • 21releasechannelhasanoxidoreductase-like domain. Proc. Natl Acad. Sci. USA 99, 12155-12160 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12155-12160
    • Baker, M.L.1
  • 16
    • 0034802465 scopus 로고    scopus 로고
    • Modeling tricks and fitting techniques for multiresolution structures
    • Wriggers, W. & Chacón, P. Modeling tricks and fitting techniques for multiresolution structures. Structure 9, 779-788 (2001).
    • (2001) Structure , vol.9 , pp. 779-788
    • Wriggers, W.1    Chacón, P.2
  • 17
    • 47749109511 scopus 로고    scopus 로고
    • Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel
    • Serysheva, I. I. et al. Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel. Proc. Natl Acad. Sci. USA 105, 9610-9615 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9610-9615
    • Serysheva, I.I.1
  • 18
    • 34848928486 scopus 로고    scopus 로고
    • Expanding spectrum of human RYR2-related disease: New electrocardiographic, structural, and genetic features
    • Bhuiyan, Z. A. et al. Expanding spectrum of human RYR2-related disease: new electrocardiographic, structural, and genetic features. Circulation 116, 1569-1576 (2007).
    • (2007) Circulation , vol.116 , pp. 1569-1576
    • Bhuiyan, Z.A.1
  • 19
    • 64549091384 scopus 로고    scopus 로고
    • Search for cardiac calcium cycling gene mutations in familial ventricular arrhythmias resembling catecholaminergic polymorphic ventricular tachycardia
    • Marjamaa, A. et al. Search for cardiac calcium cycling gene mutations in familial ventricular arrhythmias resembling catecholaminergic polymorphic ventricular tachycardia. BMC Med. Genet. 10, 12 (2009).
    • (2009) BMC Med. Genet. , vol.10 , pp. 12
    • Marjamaa, A.1
  • 20
    • 61949338001 scopus 로고    scopus 로고
    • Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle
    • Bellinger, A. M. et al. Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle. Nature Med. 15, 325-330 (2009).
    • (2009) Nature Med. , vol.15 , pp. 325-330
    • Bellinger, A.M.1
  • 21
    • 41149142599 scopus 로고    scopus 로고
    • RyR1 S-nitrosylation underlies environmental heat stroke and sudden death in Y522S RyR1 knockin mice
    • Durham, W. J. et al. RyR1 S-nitrosylation underlies environmental heat stroke and sudden death in Y522S RyR1 knockin mice. Cell 133, 53-65 (2008).
    • (2008) Cell , vol.133 , pp. 53-65
    • Durham, W.J.1
  • 23
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel(ryanodine receptor)bypoly-S-nitrosylation
    • Xu, L., Eu, J. P., Meissner, G. & Stamler, J. S. Activation of the cardiac calcium release channel(ryanodine receptor)bypoly-S-nitrosylation. Science279, 234-237(1998).
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 24
    • 33846003833 scopus 로고    scopus 로고
    • Identification of cysteines involved in S-nitrosylation S-glutathionylation and oxidationtodisulfidesinryanodine receptor type1
    • Aracena-Parks, P. et al. Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidationtodisulfidesinryanodine receptor type1.J.Biol. Chem. 281, 40354-40368 (2006).
    • (2006) J.Biol. Chem. , vol.281 , pp. 40354-40368
    • Aracena-Parks, P.1
  • 25
    • 0036514152 scopus 로고    scopus 로고
    • Regulation of calcium release by interdomain interaction within ryanodine receptors
    • Ikemoto, N. & Yamamoto, T. Regulation of calcium release by interdomain interaction within ryanodine receptors. Front. Biosci. 7, d671-d683 (2002).
    • (2002) Front. Biosci. , vol.7
    • Ikemoto, N.1    Yamamoto, T.2
  • 26
    • 0037069667 scopus 로고    scopus 로고
    • Structure ofthe inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand
    • Bosanac, I. etal. Structure ofthe inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand. Nature 420, 696-700 (2002).
    • (2002) Nature , vol.420 , pp. 696-700
    • Bosanac, I.1
  • 27
    • 12344249857 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
    • Bosanac, I. et al. Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor. Mol. Cell 17, 193-203 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 193-203
    • Bosanac, I.1
  • 28
    • 35148829933 scopus 로고    scopus 로고
    • Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1 4,5-trisphosphate receptor
    • Chan, J. et al. Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J. Mol. Biol. 373, 1269-1280 (2007).
    • (2007) J. Mol. Biol. , vol.373 , pp. 1269-1280
    • Chan, J.1
  • 30
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallo graphic software
    • McCoy,A.J.etal.Phaser crystallographicsoftware.J.Appl. Cryst.40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 31
    • 2942615325 scopus 로고    scopus 로고
    • Structureofa complex between a voltage-gated calcium channel b-subunit and an a-subunit domain
    • Van Petegem, F., Clark,K. A., Chatelain,F. C.& Minor, D. L.Jr. Structureofa complex between a voltage-gated calcium channel b-subunit and an a-subunit domain. Nature 429, 671-675 (2004).
    • (2004) Nature , vol.429 , pp. 671-675
    • Van Petegem, F.1    Clark, K.A.2    Chatelain, F.C.3    Minor Jr., D.L.4
  • 32
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nature Protocols 3, 1171-1179 (2008).
    • (2008) Nature Protocols , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 68149170539 scopus 로고    scopus 로고
    • Confidence intervals for fitting of atomic models into low-resolution densities
    • Volkmann, N. Confidence intervals for fitting of atomic models into low-resolution densities. Acta Crystallogr. D 65, 679-689 (2009).
    • (2009) Acta Crystallogr. D , vol.65 , pp. 679-689
    • Volkmann, N.1
  • 37
    • 0347380212 scopus 로고    scopus 로고
    • Docking of atomic models into reconstructions from electron microscopy
    • Volkmann, N. & Hanein, D. Docking of atomic models into reconstructions from electron microscopy. Methods Enzymol. 374, 204-225 (2003).
    • (2003) Methods Enzymol. , vol.374 , pp. 204-225
    • Volkmann, N.1    Hanein, D.2


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