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Volumn 66, Issue C, 2010, Pages 171-189

3D structure of IP 3 receptor

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EID: 77955098604     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1063-5823(10)66008-5     Document Type: Chapter
Times cited : (7)

References (66)
  • 2
    • 65549171569 scopus 로고    scopus 로고
    • Surface accessibility and conformational changes in the N-terminal domain of type-I inositol trisphosphate receptors: Studies using cysteine substitution mutagenesis
    • Anyatonwu G., Joseph S.K. Surface accessibility and conformational changes in the N-terminal domain of type-I inositol trisphosphate receptors: Studies using cysteine substitution mutagenesis. The Journal of Biological Chemistry 2009, 284:8093-8102.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 8093-8102
    • Anyatonwu, G.1    Joseph, S.K.2
  • 3
    • 0034675855 scopus 로고    scopus 로고
    • Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors
    • Boehning D., Joseph S.K. Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors. The EMBO Journal 2000, 19:5450-5459.
    • (2000) The EMBO Journal , vol.19 , pp. 5450-5459
    • Boehning, D.1    Joseph, S.K.2
  • 4
    • 0037069667 scopus 로고    scopus 로고
    • Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand
    • Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K., et al. Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand. Nature 2002, 420:696-700.
    • (2002) Nature , vol.420 , pp. 696-700
    • Bosanac, I.1    Alattia, J.R.2    Mal, T.K.3    Chan, J.4    Talarico, S.5    Tong, F.K.6
  • 6
    • 12344249857 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
    • Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K., Ikura M. Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor. Molecular Cell 2005, 17:193-203.
    • (2005) Molecular Cell , vol.17 , pp. 193-203
    • Bosanac, I.1    Yamazaki, H.2    Matsu-Ura, T.3    Michikawa, T.4    Mikoshiba, K.5    Ikura, M.6
  • 8
    • 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., Whitten A.E., Jeffries C.M., Bosanac I., Mal T.K., Ito J., et al. Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. Journal of Molecular Biology 2007, 373:1269-1280.
    • (2007) Journal of Molecular Biology , vol.373 , pp. 1269-1280
    • Chan, J.1    Whitten, A.E.2    Jeffries, C.M.3    Bosanac, I.4    Mal, T.K.5    Ito, J.6
  • 9
    • 33846202165 scopus 로고    scopus 로고
    • An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86kDa substrate
    • Chen D.H., Song J.L., Chuang D.T., Chiu W., Ludtke S.J. An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86kDa substrate. Structure 2006, 14:1711-1722.
    • (2006) Structure , vol.14 , pp. 1711-1722
    • Chen, D.H.1    Song, J.L.2    Chuang, D.T.3    Chiu, W.4    Ludtke, S.J.5
  • 10
    • 77649336015 scopus 로고    scopus 로고
    • Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics
    • Cheng L., Zhu J., Hui W.H., Zhang X., Honig B., Fang Q., et al. Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics. Journal of Molecular Biology 2010, 397:852-863.
    • (2010) Journal of Molecular Biology , vol.397 , pp. 852-863
    • Cheng, L.1    Zhu, J.2    Hui, W.H.3    Zhang, X.4    Honig, B.5    Fang, Q.6
  • 12
    • 34249930943 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptor (IP3R) and its regulators: Sometimes good and sometimes bad teamwork
    • Choe C.U., Ehrlich B.E. The inositol 1,4,5-trisphosphate receptor (IP3R) and its regulators: Sometimes good and sometimes bad teamwork. Science STKE 2006, 2006:re15.
    • (2006) Science STKE , vol.2006
    • Choe, C.U.1    Ehrlich, B.E.2
  • 17
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., Agrawal R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 2000, 406:318-322.
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 18
    • 0024432232 scopus 로고
    • Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400
    • Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N., Mikoshiba K. Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400. Nature 1989, 342:32-38.
    • (1989) Nature , vol.342 , pp. 32-38
    • Furuichi, T.1    Yoshikawa, S.2    Miyawaki, A.3    Wada, K.4    Maeda, N.5    Mikoshiba, K.6
  • 19
  • 20
    • 0346732272 scopus 로고    scopus 로고
    • Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium
    • Hamada K., Terauchi A., Mikoshiba K. Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium. The Journal of Biological Chemistry 2003, 278:52881-52889.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 52881-52889
    • Hamada, K.1    Terauchi, A.2    Mikoshiba, K.3
  • 21
    • 0000158235 scopus 로고
    • The fine structure of the Purkinje cell
    • Herndon R.M. The fine structure of the Purkinje cell. The Journal of Cell Biology 1963, 18:167-180.
    • (1963) The Journal of Cell Biology , vol.18 , pp. 167-180
    • Herndon, R.M.1
  • 22
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber A.H., Nelson W.J., Weis W.I. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell 1997, 90:871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 23
    • 34250362355 scopus 로고    scopus 로고
    • Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors
    • Iwai M., Michikawa T., Bosanac I., Ikura M., Mikoshiba K. Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors. The Journal of Biological Chemistry 2007, 282:12755-12764.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 12755-12764
    • Iwai, M.1    Michikawa, T.2    Bosanac, I.3    Ikura, M.4    Mikoshiba, K.5
  • 24
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W., Baker M.L., Jakana J., Weigele P.R., King J., Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 2008, 451:1130-1134.
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 25
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 2002, 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 26
    • 0037099206 scopus 로고    scopus 로고
    • Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 å resolution
    • Jiang Q.X., Thrower E.C., Chester D.W., Ehrlich B.E., Sigworth F.J. Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 å resolution. The EMBO Journal 2002, 21:3575-3581.
    • (2002) The EMBO Journal , vol.21 , pp. 3575-3581
    • Jiang, Q.X.1    Thrower, E.C.2    Chester, D.W.3    Ehrlich, B.E.4    Sigworth, F.J.5
  • 27
    • 0029791753 scopus 로고    scopus 로고
    • Native structure and arrangement of inositol-1,4,5-triphosphate receptor molecules in bovine cerebellar Purkinje cells as studied by quick-freeze deep-etch electron microscopy
    • Katayama E., Funahashi H., Michikawa T., SHiraishi T., Ikemoto T., Lino M., et al. Native structure and arrangement of inositol-1,4,5-triphosphate receptor molecules in bovine cerebellar Purkinje cells as studied by quick-freeze deep-etch electron microscopy. The EMBO Journal 1996, 15:4844-4851.
    • (1996) The EMBO Journal , vol.15 , pp. 4844-4851
    • Katayama, E.1    Funahashi, H.2    Michikawa, T.3    Shiraishi, T.4    Ikemoto, T.5    Lino, M.6
  • 28
    • 12444274301 scopus 로고    scopus 로고
    • Crystal structure of the potassium channel KirBac1.1 in the closed state
    • Kuo A., Gulbis J.M., Antcliff J.F., Rahman T., Lowe E.D., Zimmer J., et al. Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 2003, 300:1922-1926.
    • (2003) Science , vol.300 , pp. 1922-1926
    • Kuo, A.1    Gulbis, J.M.2    Antcliff, J.F.3    Rahman, T.4    Lowe, E.D.5    Zimmer, J.6
  • 29
    • 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 2009, 17:1505-1514.
    • (2009) Structure , vol.17 , pp. 1505-1514
    • Lobo, P.A.1    Van Petegem, F.2
  • 31
    • 40049105503 scopus 로고    scopus 로고
    • De novo backbone trace of GroEL from single particle electron cryomicroscopy
    • Ludtke S.J., Baker M.L., Chen D.H., Song J.L., Chuang D.T., Chiu W. De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 2008, 16:441-448.
    • (2008) Structure , vol.16 , pp. 441-448
    • Ludtke, S.J.1    Baker, M.L.2    Chen, D.H.3    Song, J.L.4    Chuang, D.T.5    Chiu, W.6
  • 33
    • 0025092047 scopus 로고
    • A cerebellar Purkinje cell marker P400 protein is an inositol 1,4,5-triphosphate (insP3) receptor protein. Purification and characterization of InsP3 receptor complex
    • Maeda N., Niinobe M., Mikoshiba K. A cerebellar Purkinje cell marker P400 protein is an inositol 1,4,5-triphosphate (insP3) receptor protein. Purification and characterization of InsP3 receptor complex. The EMBO Journal 1990, 9:61-67.
    • (1990) The EMBO Journal , vol.9 , pp. 61-67
    • Maeda, N.1    Niinobe, M.2    Mikoshiba, K.3
  • 36
    • 0025048773 scopus 로고
    • The ligand binding site and transduction mechanism in the inositol- 1,4,5-triphosphate receptor
    • Mignery G.A., Sudhof T.C. The ligand binding site and transduction mechanism in the inositol- 1,4,5-triphosphate receptor. The EMBO Journal 1990, 9:3893-3898.
    • (1990) The EMBO Journal , vol.9 , pp. 3893-3898
    • Mignery, G.A.1    Sudhof, T.C.2
  • 37
    • 0024449839 scopus 로고
    • Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
    • Mignery G.A., Sudhof T.C., Takei K., De Camilli P. Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature 1989, 342:192-195.
    • (1989) Nature , vol.342 , pp. 192-195
    • Mignery, G.A.1    Sudhof, T.C.2    Takei, K.3    De Camilli, P.4
  • 38
    • 34547897405 scopus 로고    scopus 로고
    • 2+ channel: From discovery to new signaling concepts
    • 2+ channel: From discovery to new signaling concepts. Journal of Neurochemistry 2007, 102:1426-1446.
    • (2007) Journal of Neurochemistry , vol.102 , pp. 1426-1446
    • Mikoshiba, K.1
  • 40
    • 0025770204 scopus 로고
    • 2+ release analysed using region-specific monoclonal antibodies
    • 2+ release analysed using region-specific monoclonal antibodies. The Biochemical Journal 1991, 277(Pt 1):125-131.
    • (1991) The Biochemical Journal , vol.277 , Issue.PART 1 , pp. 125-131
    • Nakade, S.1    Maeda, N.2    Mikoshiba, K.3
  • 41
    • 12444292684 scopus 로고    scopus 로고
    • The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins
    • Nakagawa A., Miyazaki N., Taka J., Naitow H., Ogawa A., Fujimoto Z., et al. The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. Structure 2003, 11:1227-1238.
    • (2003) Structure , vol.11 , pp. 1227-1238
    • Nakagawa, A.1    Miyazaki, N.2    Taka, J.3    Naitow, H.4    Ogawa, A.5    Fujimoto, Z.6
  • 42
    • 9144262298 scopus 로고    scopus 로고
    • The regulatory domain of the inositol 1,4,5-trisphosphate receptor is necessary to keep the channel domain closed: Possible physiological significance of specific cleavage by caspase 3
    • Nakayama T., Hattori M., Uchida K., Nakamura T., Tateishi Y., Bannai H., et al. The regulatory domain of the inositol 1,4,5-trisphosphate receptor is necessary to keep the channel domain closed: Possible physiological significance of specific cleavage by caspase 3. The Biochemical Journal 2004, 377:299-307.
    • (2004) The Biochemical Journal , vol.377 , pp. 299-307
    • Nakayama, T.1    Hattori, M.2    Uchida, K.3    Nakamura, T.4    Tateishi, Y.5    Bannai, H.6
  • 44
    • 0033976150 scopus 로고    scopus 로고
    • Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases
    • Ponting C.P. Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases. Trends in Biochemical Sciences 2000, 25:48-50.
    • (2000) Trends in Biochemical Sciences , vol.25 , pp. 48-50
    • Ponting, C.P.1
  • 45
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samso M., Feng W., Pessah I.N., Allen P.D. Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biology 2009, 7:e85.
    • (2009) PLoS Biology , vol.7
    • Samso, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 46
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M., Wagenknecht T., Allen P.D. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nature Structural and Molecular Biology 2005, 12:539-544.
    • (2005) Nature Structural and Molecular Biology , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 47
    • 9144248996 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor contains multiple cavities and L-shaped ligand-binding domains
    • Sato C., Hamada K., Ogura T., Miyazawa A., Iwasaki K., Hiroaki Y., et al. Inositol 1,4,5-trisphosphate receptor contains multiple cavities and L-shaped ligand-binding domains. Journal of Molecular Biology 2004, 336:155-164.
    • (2004) Journal of Molecular Biology , vol.336 , pp. 155-164
    • Sato, C.1    Hamada, K.2    Ogura, T.3    Miyazawa, A.4    Iwasaki, K.5    Hiroaki, Y.6
  • 48
    • 33747667565 scopus 로고    scopus 로고
    • The role of the S4-S5 linker and C-terminal tail in inositol 1,4,5-trisphosphate receptor function
    • Schug Z.T., Joseph S.K. The role of the S4-S5 linker and C-terminal tail in inositol 1,4,5-trisphosphate receptor function. The Journal of Biological Chemistry 2006, 281:24431-24440.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 24431-24440
    • Schug, Z.T.1    Joseph, S.K.2
  • 50
    • 33847194948 scopus 로고    scopus 로고
    • Single-particle electron cryomicroscopy of the ion channels in the excitation-contraction coupling junction
    • Serysheva I.I., Chiu W., Ludtke S.J. Single-particle electron cryomicroscopy of the ion channels in the excitation-contraction coupling junction. Methods in Cell Biology 2007, 79:407-435.
    • (2007) Methods in Cell Biology , vol.79 , pp. 407-435
    • Serysheva, I.I.1    Chiu, W.2    Ludtke, S.J.3
  • 53
    • 2942694513 scopus 로고    scopus 로고
    • Functional properties of the Drosophila melanogaster inositol 1,4,5-trisphosphate receptor mutants
    • Srikanth S., Wang Z., Tu H., Nair S., Mathew M.K., Hasan G., et al. Functional properties of the Drosophila melanogaster inositol 1,4,5-trisphosphate receptor mutants. Biophysical Journal 2004, 86:3634-3646.
    • (2004) Biophysical Journal , vol.86 , pp. 3634-3646
    • Srikanth, S.1    Wang, Z.2    Tu, H.3    Nair, S.4    Mathew, M.K.5    Hasan, G.6
  • 54
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • Stewart A., Grigorieff N. Noise bias in the refinement of structures derived from single particles. Ultramicroscopy 2004, 102:67-84.
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 55
    • 0028348910 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells
    • Takei K., Mignery G.A., Mugnaini E., Sudhof T.C., De Camilli P. Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells. Neuron 1994, 12:327-342.
    • (1994) Neuron , vol.12 , pp. 327-342
    • Takei, K.1    Mignery, G.A.2    Mugnaini, E.3    Sudhof, T.C.4    De Camilli, P.5
  • 59
    • 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. Biophysical Journal 2004, 87:2335-2351.
    • (2004) Biophysical Journal , vol.87 , pp. 2335-2351
    • Welch, W.1    Rheault, S.2    West, D.J.3    Williams, A.J.4
  • 60
    • 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. Quarterly Reviews of Biophysics 2001, 34:61-104.
    • (2001) Quarterly Reviews of Biophysics , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 63
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu X., Jin L., Zhou Z.H. 3.88 å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 2008, 453:415-419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 66
    • 0034814786 scopus 로고    scopus 로고
    • Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus
    • Zhou Z.H., Baker M.L., Jiang W., Dougherty M., Jakana J., Dong G., et al. Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nature Structural Biology 2001, 8:868-873.
    • (2001) Nature Structural Biology , vol.8 , pp. 868-873
    • Zhou, Z.H.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Jakana, J.5    Dong, G.6


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