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Volumn 287, Issue 34, 2012, Pages 28480-28494

Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator

Author keywords

[No Author keywords available]

Indexed keywords

CHANNEL ACTIVITY; CHANNEL GATING; CHANNEL OPEN PROBABILITY; CONFORMATIONAL CHANGE; CONFORMATIONAL EQUILIBRIUM; CONFORMATIONAL FLUCTUATIONS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATORS; DOCKING SIMULATIONS; NMR ASSIGNMENT; NMR DATA; NUCLEOTIDE-BINDING DOMAIN; REGULATORY REGIONS;

EID: 84865234037     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.371138     Document Type: Article
Times cited : (40)

References (69)
  • 5
    • 0035896542 scopus 로고    scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl- Channel by its R domain
    • Ostedgaard, L. S., Baldursson, O., and Welsh, M. J. (2001) Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by its R domain. J. Biol. Chem. 276, 7689-7692
    • (2001) J. Biol. Chem. , vol.276 , pp. 7689-7692
    • Ostedgaard, L.S.1    Baldursson, O.2    Welsh, M.J.3
  • 7
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • Hallows, K. R., Raghuram, V., Kemp, B. E., Witters, L. A., and Foskett, J. K. (2000) Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. J. Clin. Invest. 105, 1711-1721 (Pubitemid 30421752)
    • (2000) Journal of Clinical Investigation , vol.105 , Issue.12 , pp. 1711-1721
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Witters, L.A.4    Foskett, J.K.5
  • 8
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • DOI 10.1016/S1097-2765(02)00576-2
    • Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., and Hunt, J. F. (2002) ATP binding to the motor domain from anABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (Pubitemid 34876568)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 9
    • 23844483240 scopus 로고    scopus 로고
    • Phosphorylation of CFTR by PKA promotes binding of the regulatory domain
    • DOI 10.1038/sj.emboj.7600747
    • Chappe, V., Irvine, T., Liao, J., Evagelidis, A., and Hanrahan, J. W. (2005) Phosphorylation of CFTR by PKA promotes binding of the regulatory domain. EMBO J. 24, 2730-2740 (Pubitemid 41170023)
    • (2005) EMBO Journal , vol.24 , Issue.15 , pp. 2730-2740
    • Chappe, V.1    Irvine, T.2    Liao, J.3    Evagelidis, A.4    Hanrahan, J.W.5
  • 10
    • 33750222000 scopus 로고    scopus 로고
    • In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer
    • DOI 10.1038/sj.emboj.7601373, PII 7601373
    • Mense, M., Vergani, P., White, D. M., Altberg, G., Nairn, A. C., and Gadsby, D. C. (2006) In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. EMBO J. 25, 4728-4739 (Pubitemid 44607019)
    • (2006) EMBO Journal , vol.25 , Issue.20 , pp. 4728-4739
    • Mense, M.1    Vergani, P.2    White, D.M.3    Altberg, G.4    Nairn, A.C.5    Gadsby, D.C.6
  • 11
    • 70349847830 scopus 로고    scopus 로고
    • Molecular models of the open and closed states of the whole human CFTR protein
    • Mornon, J. P., Lehn, P., and Callebaut, I. (2009) Molecular models of the open and closed states of the whole human CFTR protein. Cell Mol. Life Sci. 66, 3469-3486
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 3469-3486
    • Mornon, J.P.1    Lehn, P.2    Callebaut, I.3
  • 12
    • 65749102092 scopus 로고    scopus 로고
    • Gating of the CFTR Cl- Channel by ATP-driven nucleotide-binding domain dimerization
    • Hwang, T. C., and Sheppard, D. N. (2009) Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerization. J. Physiol. 587, 2151-2161
    • (2009) J. Physiol. , vol.587 , pp. 2151-2161
    • Hwang, T.C.1    Sheppard, D.N.2
  • 13
    • 0036258208 scopus 로고    scopus 로고
    • Cystic fibrosis: A worldwide analysis of CFTR mutations - Correlation with incidence data and application to screening
    • DOI 10.1002/humu.10041
    • Bobadilla, J. L., Macek, M., Jr., Fine, J. P., and Farrell, P. M. (2002) Cystic fibrosis: A worldwide analysis of CFTR mutations-correlation with incidence data and application to screening. Hum. Mutat. 19, 575-606 (Pubitemid 34556480)
    • (2002) Human Mutation , vol.19 , Issue.6 , pp. 575-606
    • Bobadilla, J.L.1    Macek Jr., M.2    Fine, J.P.3    Farrell, P.M.4
  • 14
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • DOI 10.1016/0092-8674(93)90353-R
    • Welsh, M. J., and Smith, A. E. (1993) Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73, 1251-1254 (Pubitemid 23201140)
    • (1993) Cell , vol.73 , Issue.7 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 15
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G. M., Anderson, M. P., Amara, J. F., Marshall, J., Smith, A. E., and Welsh, M. J. (1992) Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358, 761-764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 16
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • DOI 10.1074/jbc.271.2.635
    • Sato, S., Ward, C. L., Krouse, M. E., Wine, J. J., and Kopito, R. R. (1996) Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271, 635-638 (Pubitemid 26034907)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.2 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 17
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis ΔF508 mutation using STE6-CFTR chimeras in yeast
    • DOI 10.1016/0092-8674(93)90233-G
    • Teem, J. L., Berger, H. A., Ostedgaard, L. S., Rich, D. P., Tsui, L. C., and Welsh, M. J. (1993) Identification of revertants for the cystic fibrosis ΔF508 mutation using STE6-CFTR chimeras in yeast. Cell 73, 335-346 (Pubitemid 23123311)
    • (1993) Cell , vol.73 , Issue.2 , pp. 335-346
    • Teem, J.L.1    Berger, H.A.2    Ostedgaard, L.S.3    Rich, D.P.4    Tsui, L.-C.5    Welsh, M.J.6
  • 18
    • 38349050413 scopus 로고    scopus 로고
    • Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation
    • Pissarra, L. S., Farinha, C. M., Xu, Z., Schmidt, A., Thibodeau, P. H., Cai, Z., Thomas, P. J., Sheppard, D. N., and Amaral, M. D. (2008) Solubilizing mutations used to crystallize one CFTR domain attenuate the trafficking and channel defects caused by the major cystic fibrosis mutation. Chem. Biol. 15, 62-69
    • (2008) Chem. Biol. , vol.15 , pp. 62-69
    • Pissarra, L.S.1    Farinha, C.M.2    Xu, Z.3    Schmidt, A.4    Thibodeau, P.H.5    Cai, Z.6    Thomas, P.J.7    Sheppard, D.N.8    Amaral, M.D.9
  • 21
    • 0031915434 scopus 로고    scopus 로고
    • Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTR
    • DOI 10.1038/nsb0398-180
    • Zhang, F., Kartner, N., and Lukacs, G. L. (1998) Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTR. Nat. Struct. Biol. 5, 180-183 (Pubitemid 28113747)
    • (1998) Nature Structural Biology , vol.5 , Issue.3 , pp. 180-183
    • Zhang, F.1    Kartner, N.2    Lukacs, G.L.3
  • 28
    • 84856629737 scopus 로고    scopus 로고
    • CFTR: Folding, misfolding, and correcting the ΔF508 conformational defect
    • Lukacs, G. L., and Verkman, A. S. (2012) CFTR: Folding, misfolding, and correcting the ΔF508 conformational defect. Trends Mol. Med. 18, 81-91
    • (2012) Trends Mol. Med. , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 30
    • 80052326351 scopus 로고    scopus 로고
    • NMR spectroscopy to study the dynamics and interactions of CFTR
    • Kanelis, V., Chong, P. A., and Forman-Kay, J. D. (2011) NMR spectroscopy to study the dynamics and interactions of CFTR. Methods Mol. Biol. 741, 377-403
    • (2011) Methods Mol. Biol. , vol.741 , pp. 377-403
    • Kanelis, V.1    Chong, P.A.2    Forman-Kay, J.D.3
  • 31
    • 75649088951 scopus 로고    scopus 로고
    • NMR evidence for differential phosphorylation-dependent interactions in WT and ΔF508 CFTR
    • Kanelis, V., Hudson, R. P., Thibodeau, P. H., Thomas, P. J., and Forman-Kay, J. D. (2010) NMR evidence for differential phosphorylation-dependent interactions in WT and ΔF508 CFTR. EMBO J. 29, 263-277
    • (2010) EMBO J. , vol.29 , pp. 263-277
    • Kanelis, V.1    Hudson, R.P.2    Thibodeau, P.H.3    Thomas, P.J.4    Forman-Kay, J.D.5
  • 32
    • 77957302946 scopus 로고    scopus 로고
    • Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1
    • Protasevich, I., Yang, Z., Wang, C., Atwell, S., Zhao, X., Emtage, S., Wetmore, D., Hunt, J. F., and Brouillette, C. G. (2010) Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. Protein Sci. 19, 1917-1931
    • (2010) Protein Sci. , vol.19 , pp. 1917-1931
    • Protasevich, I.1    Yang, Z.2    Wang, C.3    Atwell, S.4    Zhao, X.5    Emtage, S.6    Wetmore, D.7    Hunt, J.F.8    Brouillette, C.G.9
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 34249765651 scopus 로고
    • NMR view: A computer program for the visualization and analysis ofNMRdata
    • Johnson, B. A., and Blevins, R. A. (1994) NMR view: A computer program for the visualization and analysis ofNMRdata. J. Biomol.NMR4, 603-614
    • (1994) J. Biomol.NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 35
    • 0004040543 scopus 로고    scopus 로고
    • version 3, University of California, San Francisco
    • Goddard, T. D., and Kneller, D. G. (2008) Sparky 3, version 3, University of California, San Francisco
    • (2008) Sparky 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 36
    • 0033032816 scopus 로고    scopus 로고
    • 1HN-detected triple resonance TROSY-based experiments
    • DOI 10.1023/A:1008329230975
    • Yang, D., and Kay, L. E. (1999) Improved 1HN-detected triple resonance TROSY-based experiments. J. Biomol. NMR 13, 3-10 (Pubitemid 29089234)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.1 , pp. 3-10
    • Yang, D.1    Kay, L.E.2
  • 39
  • 41
    • 84857607825 scopus 로고    scopus 로고
    • Accelrys 2.5 Ed., Accelrys Software, Inc., San Diego
    • Accelrys (2005-2009) Discovery Studio Modeling Environment, 2.5 Ed., Accelrys Software, Inc., San Diego
    • (2005) Discovery Studio Modeling Environment
  • 42
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J., van der Spoel, D., and van Drunen, R. (1995) GROMACS: A message-passing parallel molecular dynamics implementation. Comp. Phys. Comm. 91, 43-56
    • (1995) Comp. Phys. Comm. , vol.91 , pp. 43-56
    • Berendsen, H.J.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 43
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 45
    • 41549127613 scopus 로고    scopus 로고
    • A temperature predictor for parallel tempering simulations
    • Patriksson, A., and van der Spoel, D. (2008) A temperature predictor for parallel tempering simulations. Phys. Chem. Chem. Phys. 10, 2073-2077
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2073-2077
    • Patriksson, A.1    Van Der Spoel, D.2
  • 46
    • 0347784245 scopus 로고
    • Quiet high-resolution computer models of a plasma
    • Hockney, R. W., Goel, S. P., and Eastwood, J. W. (1974) Quiet high-resolution computer models of a plasma. J. Comput. Phys. 14, 148-158
    • (1974) J. Comput. Phys. , vol.14 , pp. 148-158
    • Hockney, R.W.1    Goel, S.P.2    Eastwood, J.W.3
  • 47
    • 33846823909 scopus 로고
    • Particle mesh Ewald: AnW log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: AnW log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 51
    • 84865248678 scopus 로고    scopus 로고
    • Schrodinger, LLC. version 9.1, Schrodinger, New York
    • Schrodinger, LLC. (2010) Maestro, version 9.1, Schrodinger, New York
    • (2010) Maestro
  • 52
    • 33847770470 scopus 로고    scopus 로고
    • Multiscale modeling of nucleosome dynamics
    • DOI 10.1529/biophysj.106.094805
    • Sharma, S., Ding, F., and Dokholyan, N. V. (2007) Multiscale modeling of nucleosome dynamics. Biophys. J. 92, 1457-1470 (Pubitemid 46393459)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1457-1470
    • Sharma, S.1    Ding, F.2    Dokholyan, N.V.3
  • 53
    • 84865216153 scopus 로고    scopus 로고
    • Schrodinger Suite 2010 Induced Fit Docking protocol
    • Schrodinger, LLC version 5.6, New York, NY
    • Schrodinger, LLC (2010) Schrodinger Suite 2010 Induced Fit Docking protocol, Glide, version 5.6, New York, NY
    • (2010) Glide
  • 54
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 55
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 56
    • 77954591521 scopus 로고    scopus 로고
    • C terminus of nucleotide binding domain 1 contains critical features for cystic fibrosis transmembrane conductance regulator trafficking and activation
    • Billet, A., Melin, P., Jollivet, M., Mornon, J. P., Callebaut, I., and Becq, F. (2010) C terminus of nucleotide binding domain 1 contains critical features for cystic fibrosis transmembrane conductance regulator trafficking and activation. J. Biol. Chem. 285, 22132-22140
    • (2010) J. Biol. Chem. , vol.285 , pp. 22132-22140
    • Billet, A.1    Melin, P.2    Jollivet, M.3    Mornon, J.P.4    Callebaut, I.5    Becq, F.6
  • 57
    • 0032515182 scopus 로고    scopus 로고
    • Phosphorylation site independent single R-domain mutations affect CFTR channel activity
    • DOI 10.1016/S0014-5793(98)01351-9, PII S0014579398013519
    • Wei, L., Vankeerberghen, A., Cuppens, H., Droogmans, G., Cassiman, J. J., and Nilius, B. (1998) Phosphorylation site-independent single R-domain mutations affect CFTR channel activity. FEBS Lett. 439, 121-126 (Pubitemid 28537877)
    • (1998) FEBS Letters , vol.439 , Issue.1-2 , pp. 121-126
    • Wei, L.1    Vankeerberghen, A.2    Cuppens, H.3    Droogmans, G.4    Cassiman, J.-J.5    Nilius, B.6
  • 58
    • 0032538411 scopus 로고    scopus 로고
    • Characterization of mutations located in exon 18 of the CFTR gene
    • DOI 10.1016/S0014-5793(98)01042-4, PII S0014579398010424
    • Vankeerberghen, A., Wei, L., Teng, H., Jaspers, M., Cassiman, J. J., Nilius, B., and Cuppens, H. (1998) Characterization of mutations located in exon 18 of the CFTR gene. FEBS Lett. 437, 1-4 (Pubitemid 28498229)
    • (1998) FEBS Letters , vol.437 , Issue.1-2 , pp. 1-4
    • Vankeerberghen, A.1    Wei, L.2    Teng, H.3    Jaspers, M.4    Cassiman, J.-J.5    Nilius, B.6    Cuppens, H.7
  • 59
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation
    • DOI 10.1110/ps.062465306
    • Marsh, J. A., Singh, V. K., Jia, Z., and Forman-Kay, J. D. (2006) Sensitivity of secondary structure propensities to sequence differences between α-and γ-synuclein: Implications for fibrillation. Protein Sci. 15, 2795-2804 (Pubitemid 44833760)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 62
    • 33745088619 scopus 로고    scopus 로고
    • Use of an induced fit receptor structure in virtual screening
    • DOI 10.1111/j.1747-0285.2005.00327.x
    • Sherman, W., Beard, H. S., and Farid, R. (2006) Use of an induced fit receptor structure in virtual screening. Chem. Biol. Drug Des. 67, 83-84 (Pubitemid 43881391)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 83-84
    • Sherman, W.1    Beard, H.S.2    Farid, R.3
  • 65
    • 12344263101 scopus 로고    scopus 로고
    • Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    • Csanády, L., Chan, K. W., Nairn, A. C., and Gadsby, D. C. (2005) Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain. J. Gen. Physiol. 125, 43-55
    • (2005) J. Gen. Physiol. , vol.125 , pp. 43-55
    • Csanády, L.1    Chan, K.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 67
    • 80052340812 scopus 로고    scopus 로고
    • The role of protein conformational fluctuations in allostery, function, and evolution
    • Wrabl, J. O., Gu, J., Liu, T., Schrank, T. P., Whitten, S. T., and Hilser, V. J. (2011) The role of protein conformational fluctuations in allostery, function, and evolution. Biophys. Chem. 159, 129-141
    • (2011) Biophys. Chem. , vol.159 , pp. 129-141
    • Wrabl, J.O.1    Gu, J.2    Liu, T.3    Schrank, T.P.4    Whitten, S.T.5    Hilser, V.J.6
  • 68
    • 84865268467 scopus 로고    scopus 로고
    • December 29, Patent WO 2010/151747 A1
    • Chang, P., and Ghosh, S. (December 29, 2010) Patent WO 2010/151747 A1
    • (2010)
    • Chang, P.1    Ghosh, S.2


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