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Volumn 287, Issue 21, 2012, Pages 17232-17240

Calcium-induced conformational changes in C-terminal tail of polycystin-2 are necessary for channel gating

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; AUTOSOMAL DOMINANTS; C-TERMINAL TAIL; CHANNEL GATING; CHANNEL PORE; CONFORMATIONAL CHANGE; CYTOPLASMIC DOMAINS; CYTOPLASMIC TAIL; DOMINANT NEGATIVE; EF-HAND; INTER-ATOMIC DISTANCES; KIDNEY CELLS; MOLECULAR BASIS; OVER-EXPRESSION; POLYCYSTIC KIDNEY DISEASE; RADIUS OF GYRATION; SINGLE-CHANNEL; SMALL ANGLE X-RAY SCATTERING; TRANSIENT RECEPTOR POTENTIAL CHANNELS;

EID: 84861217550     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.354613     Document Type: Article
Times cited : (42)

References (37)
  • 1
    • 34047276812 scopus 로고    scopus 로고
    • Autosomal dominant polycystic kidney disease
    • DOI 10.1016/S0140-6736(07)60601-1, PII S0140673607606011
    • Torres, V. E., Harris, P. C., and Pirson, Y. (2007) Autosomal dominant polycystic kidney disease. Lancet 369, 1287-1301 (Pubitemid 46552051)
    • (2007) Lancet , vol.369 , Issue.9569 , pp. 1287-1301
    • Torres, V.E.1    Harris, P.C.2    Pirson, Y.3
  • 2
    • 0033972998 scopus 로고    scopus 로고
    • Molecular genetics and mechanism of autosomal dominant polycystic kidney disease
    • DOI 10.1006/mgme.1999.2943
    • Wu, G., and Somlo, S. (2000) Molecular genetics and mechanism of autosomal dominant polycystic kidney disease. Mol. Genet. Metab. 69, 1-15 (Pubitemid 30097298)
    • (2000) Molecular Genetics and Metabolism , vol.69 , Issue.1 , pp. 1-15
    • Wu, G.1    Somlo, S.2
  • 3
    • 79959794812 scopus 로고    scopus 로고
    • Structural biology of TRP channels
    • Li, M., Yu, Y., and Yang, J. (2011) Structural biology of TRP channels. Adv. Exp. Med. Biol. 704, 1-23
    • (2011) Adv. Exp. Med. Biol. , vol.704 , pp. 1-23
    • Li, M.1    Yu, Y.2    Yang, J.3
  • 4
    • 57649114598 scopus 로고    scopus 로고
    • Domain mapping of the polycystin-2 C-terminal tail using de novo molecular modeling and biophysical analysis
    • Ćelić, A., Petri, E. T., Demeler, B., Ehrlich, B. E., and Boggon, T. J. (2008) Domain mapping of the polycystin-2 C-terminal tail using de novo molecular modeling and biophysical analysis. J. Biol. Chem. 283, 28305-28312
    • (2008) J. Biol. Chem. , vol.283 , pp. 28305-28312
    • Ćelić, A.1    Petri, E.T.2    Demeler, B.3    Ehrlich, B.E.4    Boggon, T.J.5
  • 9
    • 0030909957 scopus 로고    scopus 로고
    • PKD1 interacts with PKD2 through a probable coiled-coil domain
    • DOI 10.1038/ng0697-179
    • Qian, F., Germino, F. J., Cai, Y., Zhang, X., Somlo, S., and Germino, G. G. (1997) PKD1 interacts with PKD2 through a probable coiled-coil domain. Nat. Genet. 16, 179-183 (Pubitemid 27240617)
    • (1997) Nature Genetics , vol.16 , Issue.2 , pp. 179-183
    • Qian, F.1    Germino, F.J.2    Cai, Y.3    Zhang, X.4    Somlo, S.5    Germino, G.G.6
  • 10
    • 84856032648 scopus 로고    scopus 로고
    • Crystal structure and characterization of coiled-coil domain of the transient receptor potential channel PKD2L1
    • Molland, K. L., Paul, L. N., and Yernool, D. A. (2012) Crystal structure and characterization of coiled-coil domain of the transient receptor potential channel PKD2L1. Biochim. Biophys. Acta 1824, 413-421
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 413-421
    • Molland, K.L.1    Paul, L.N.2    Yernool, D.A.3
  • 13
    • 79956300184 scopus 로고    scopus 로고
    • A single amino acid residue constitutes the third dimerization domain essential for the assembly and function of the tetrameric polycystin-2 (TRPP2) channel
    • Feng, S., Rodat-Despoix, L., Delmas, P., and Ong, A. C. (2011) A single amino acid residue constitutes the third dimerization domain essential for the assembly and function of the tetrameric polycystin-2 (TRPP2) channel. J. Biol. Chem. 286, 18994-19000
    • (2011) J. Biol. Chem. , vol.286 , pp. 18994-19000
    • Feng, S.1    Rodat-Despoix, L.2    Delmas, P.3    Ong, A.C.4
  • 17
    • 72149113587 scopus 로고    scopus 로고
    • The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement
    • Kobori, T., Smith, G. D., Sandford, R., and Edwardson, J. M. (2009) The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement. J. Biol. Chem. 284, 35507-35513
    • (2009) J. Biol. Chem. , vol.284 , pp. 35507-35513
    • Kobori, T.1    Smith, G.D.2    Sandford, R.3    Edwardson, J.M.4
  • 20
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 23
    • 38649117291 scopus 로고    scopus 로고
    • Monte Carlo analysis of sedimentation experiments
    • Demeler, B., and Brookes, E. (2007) Monte Carlo analysis of sedimentation experiments. Colloid Polym. Sci. 286, 129-137
    • (2007) Colloid Polym. Sci. , vol.286 , pp. 129-137
    • Demeler, B.1    Brookes, E.2
  • 24
    • 0031982612 scopus 로고    scopus 로고
    • Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation
    • Demeler, B., and Saber, H. (1998) Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation. Biophys. J. 74, 444-454 (Pubitemid 28041772)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 444-454
    • Demeler, B.1    Saber, H.2
  • 25
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • DOI 10.1016/j.ab.2004.08.039, PII S0003269704007225
    • Demeler, B., and van Holde, K. E. (2004) Sedimentation velocity analysis of highly heterogeneous systems. Anal. Biochem. 335, 279-288 (Pubitemid 39535193)
    • (2004) Analytical Biochemistry , vol.335 , Issue.2 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2
  • 26
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 27
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid abinitio shape determination in small-angle scattering
    • Franke, D., and Svergun, D. I. (2009) DAMMIF, a program for rapid abinitio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 28
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • DOI 10.1107/S0021889800014126
    • Kozin, M., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41 (Pubitemid 32151714)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.1 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 29
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D. I., Barberato, C., and Koch, M. H. (1995) CRYSOL. A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 30
    • 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
  • 32
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 35
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam, C. D., Hammel, M., Hura, G. L., and Tainer, J. A. (2007) X-ray solution scattering (SAXS) combined with crystallography and computation. Defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40, 191-285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 36
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.