메뉴 건너뛰기




Volumn 76, Issue 6, 1999, Pages 2887-2898

The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 32; PROLINE;

EID: 0033063884     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77444-8     Document Type: Article
Times cited : (97)

References (40)
  • 1
    • 0026755609 scopus 로고
    • Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains
    • Ballesteros, J. A., and H. Weinstein. 1992. Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains. Biophys. J. 62:107-109.
    • (1992) Biophys. J. , vol.62 , pp. 107-109
    • Ballesteros, J.A.1    Weinstein, H.2
  • 2
    • 77957055780 scopus 로고
    • Integrated methods for modeling G-protein coupled receptors
    • Ballesteros, J. A., and H. Weinstein. 1995. Integrated methods for modeling G-protein coupled receptors. Methods Neurosci. 25:366-428.
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 3
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J., and J. M. Thornton. 1988. Helix geometry in proteins. J. Mol. Biol. 201:601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 5
    • 0030976035 scopus 로고    scopus 로고
    • Monovalent cation permeation through the connexin40 gap junction channel. Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions BR, Cl, F, acetate, aspartate, glutamate and NO3
    • Beblo, D. A., and R. D. Veenstra. 1997. Monovalent cation permeation through the connexin40 gap junction channel. Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions BR, Cl, F, acetate, aspartate, glutamate and NO3. J. Gen. Physiol. 109:509-522.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 509-522
    • Beblo, D.A.1    Veenstra, R.D.2
  • 7
    • 0017682970 scopus 로고
    • Gap junction strucutres. I. Correlated electron microscopy and x-ray diffraction
    • Casper, D. L., D. A. Goodenough, L. Makowski, and W. C. Phillips. 1977. Gap junction strucutres. I. Correlated electron microscopy and x-ray diffraction. J. Cell Biol. 74:605-628.
    • (1977) J. Cell Biol. , vol.74 , pp. 605-628
    • Casper, D.L.1    Goodenough, D.A.2    Makowski, L.3    Phillips, W.C.4
  • 8
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the b2 adrenergic receptor
    • Gether, U., S. Lin, P. Ghanouni, J. A. Ballesteros, H. Weinstein, and B. K. Kobilka. 1997. Agonists induce conformational changes in transmembrane domains III and VI of the b2 adrenergic receptor. EMBO J. 16(22):6737-6747.
    • (1997) EMBO J. , vol.16 , Issue.22 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 9
    • 0021755525 scopus 로고
    • Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins
    • Gray, T. M., and B. W. Matthews. 1984. Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins. J. Mol. Biol. 175(1):75-81.
    • (1984) J. Mol. Biol. , vol.175 , Issue.1 , pp. 75-81
    • Gray, T.M.1    Matthews, B.W.2
  • 10
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., T. A. Ceska, K. H. Downing, J. M. Baldwin, and R. Henderson. 1996. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259(3):393-421.
    • (1996) J. Mol. Biol. , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 11
    • 0030055923 scopus 로고    scopus 로고
    • Conformational memories and the exploration of biologically relevant peptide conformations: An illustration for the gonadotropin-releasing hormone
    • Guamieri, F., and H. Weinstein. 1996. Conformational memories and the exploration of biologically relevant peptide conformations: an illustration for the gonadotropin-releasing hormone. J. Am. Chem. Soc. 118: 5580-5589.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5580-5589
    • Guamieri, F.1    Weinstein, H.2
  • 12
    • 84986505816 scopus 로고
    • Conformational memories and a simulated annealing program that learns: Application to LTB4
    • Guarnieri, F., and S. R. Wilson. 1995. Conformational memories and a simulated annealing program that learns: application to LTB4. J. Comput. Chem. 16(5):648-653.
    • (1995) J. Comput. Chem. , vol.16 , Issue.5 , pp. 648-653
    • Guarnieri, F.1    Wilson, S.R.2
  • 14
    • 26444479778 scopus 로고
    • Optimization by simulated annealing
    • Kirkpatrick, S., C. D. Gelatt, and M. P. Vecchi. 1983. Optimization by simulated annealing. Science. 220:671-680.
    • (1983) Science. , vol.220 , pp. 671-680
    • Kirkpatrick, S.1    Gelatt, C.D.2    Vecchi, M.P.3
  • 15
    • 0028600609 scopus 로고
    • Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor
    • Luo, X., D. Zhang, and H. Weinstein. 1993. Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor. Protein Eng. 7:1441-1448.
    • (1993) Protein Eng. , vol.7 , pp. 1441-1448
    • Luo, X.1    Zhang, D.2    Weinstein, H.3
  • 16
    • 0017640572 scopus 로고
    • Gap junction structures. II. Analysis of the x-ray diffraction data
    • Makowski, L., D. L. Casper, D. A. Goodenough, and W. C. Phillips. 1977. Gap junction structures. II. Analysis of the x-ray diffraction data. J. Cell Biol. 74:629-645.
    • (1977) J. Cell Biol. , vol.74 , pp. 629-645
    • Makowski, L.1    Casper, D.L.2    Goodenough, D.A.3    Phillips, W.C.4
  • 17
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor, M. J., S. A. Islam, and M. J. Sternberg. 1987. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 198(2):295-310.
    • (1987) J. Mol. Biol. , vol.198 , Issue.2 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.3
  • 19
    • 0028362273 scopus 로고
    • Gap junction channels: Distinct voltage-sensitive and -insensitive conductance states
    • Moreno, A. P., M. B. Rook, G. I. Fishman, and D. C. Spray. 1994. Gap junction channels: distinct voltage-sensitive and -insensitive conductance states. Biophys. J. 67:113-119.
    • (1994) Biophys. J. , vol.67 , pp. 113-119
    • Moreno, A.P.1    Rook, M.B.2    Fishman, G.I.3    Spray, D.C.4
  • 20
    • 0030777706 scopus 로고    scopus 로고
    • Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease
    • Oh, S., Y. Ri, M. V. L. Bennett, E. B. Trexler, V. K. Verselis, and T. A. Bargiello. 1997. Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease. Neuron. 19: 927-938.
    • (1997) Neuron. , vol.19 , pp. 927-938
    • Oh, S.1    Ri, Y.2    Bennett, M.V.L.3    Trexler, E.B.4    Verselis, V.K.5    Bargiello, T.A.6
  • 21
    • 0024504201 scopus 로고
    • The dynamic properties of melittin in solution. Investigations by NMR and molecular dynamics
    • Pastore, A., T. S. Harvey, C. E. Dempsey, and I. D. Campbell. 1989. The dynamic properties of melittin in solution. Investigations by NMR and molecular dynamics. Eur. Biophys. J. 16(6):363-367.
    • (1989) Eur. Biophys. J. , vol.16 , Issue.6 , pp. 363-367
    • Pastore, A.1    Harvey, T.S.2    Dempsey, C.E.3    Campbell, I.D.4
  • 22
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, and E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277(5332): 1676-1681.
    • (1997) Science. , vol.277 , Issue.5332 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 23
    • 0023404610 scopus 로고
    • Proline-induced constraints in alpha-helices
    • Piela, L., G. Nemethy, and H. A. Scheraga. 1987. Proline-induced constraints in alpha-helices. Biopolymers. 26:1587-1600.
    • (1987) Biopolymers. , vol.26 , pp. 1587-1600
    • Piela, L.1    Nemethy, G.2    Scheraga, H.A.3
  • 24
    • 0026666944 scopus 로고
    • Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32
    • Rubin, J. B., V. K. Verselis, M. V. L. Bennett, and T. A. Bargiello. 1992. Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32. Biophys. J. 62:183-195.
    • (1992) Biophys. J. , vol.62 , pp. 183-195
    • Rubin, J.B.1    Verselis, V.K.2    Bennett, M.V.L.3    Bargiello, T.A.4
  • 26
    • 0026537558 scopus 로고
    • Proline residues in transmembrane helices of channel and transport proteins: A molecular modelling study
    • Sansom, M. S. 1992. Proline residues in transmembrane helices of channel and transport proteins: a molecular modelling study. Protein Eng. 5:53-60.
    • (1992) Protein Eng. , vol.5 , pp. 53-60
    • Sansom, M.S.1
  • 27
    • 0031959735 scopus 로고    scopus 로고
    • A missense mutation in the human connexin50 gene underlies autosomal dominant "zonular pulverulent" cataract, on chromosome 1q
    • Shiels, A., D. Mackay, A. Ionides, A. Moore, and S. Bhattacharya. 1998. A missense mutation in the human connexin50 gene underlies autosomal dominant "zonular pulverulent" cataract, on chromosome 1q. Am. J. Hum. Genet. 62:526-532.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 526-532
    • Shiels, A.1    Mackay, D.2    Ionides, A.3    Moore, A.4    Bhattacharya, S.5
  • 28
    • 0027442575 scopus 로고
    • Identification of a proline residue as a transduction element involved in voltage gating of gap junctions
    • Suchyna, T. M., L. X. Xu, F. Gao, C. R. Fourtner, and B. J. Nicholson. 1993. Identification of a proline residue as a transduction element involved in voltage gating of gap junctions. Nature. 365:847-849.
    • (1993) Nature. , vol.365 , pp. 847-849
    • Suchyna, T.M.1    Xu, L.X.2    Gao, F.3    Fourtner, C.R.4    Nicholson, B.J.5
  • 29
    • 0031024656 scopus 로고    scopus 로고
    • Projection structure of a gap junction membrane channel at 7 a resolution
    • Unger, V. M., N. M. Kumar, N. B. Gilula, and M. Yeager. 1997. Projection structure of a gap junction membrane channel at 7 A resolution. Nature Struct. Biol. 4:39-43.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 39-43
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 30
    • 0033582686 scopus 로고    scopus 로고
    • Three dimensional structure of a recombinant gap junction membrane channel
    • Unger, V. M., N. M. Kumar, N. B. Gilula, and M. Yeager. 1999. Three dimensional structure of a recombinant gap junction membrane channel. Science. 283:1176-1180.
    • (1999) Science. , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 31
    • 0021139243 scopus 로고
    • Two configurations of a channel-forming membrane protein
    • Unwin, P. N., and P. D. Ennis. 1984. Two configurations of a channel-forming membrane protein. Nature. 307:609-613.
    • (1984) Nature. , vol.307 , pp. 609-613
    • Unwin, P.N.1    Ennis, P.D.2
  • 32
    • 0028299152 scopus 로고
    • Opposite voltage gating polarities of two closely related connexins
    • Verselis, V. K., C. S. Ginter, and T. A. Bargiello. 1994. Opposite voltage gating polarities of two closely related connexins. Nature. 368:348-351.
    • (1994) Nature. , vol.368 , pp. 348-351
    • Verselis, V.K.1    Ginter, C.S.2    Bargiello, T.A.3
  • 33
    • 0030986975 scopus 로고    scopus 로고
    • Monovalent ion selectivity sequences of the rat connexin43 gap junction channel
    • Wang, H. Z., and Veenstra. 1997. Monovalent ion selectivity sequences of the rat connexin43 gap junction channel. J. Gen. Physiol. 109:491-507.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 491-507
    • Wang, H.Z.1    Veenstra2
  • 34
    • 0032476578 scopus 로고    scopus 로고
    • Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts
    • White, T. W., D. A. Goodenough, and D. L. Paul. 1998. Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts. J. Cell Biol. 143:815-825.
    • (1998) J. Cell Biol. , vol.143 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3
  • 35
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamic role?
    • Williams, K. A., and C. M. Deber. 1991. Proline residues in transmembrane helices: structural or dynamic role? Biochemistry. 30(37): 8919-8923.
    • (1991) Biochemistry , vol.30 , Issue.37 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 36
    • 0025801502 scopus 로고
    • Conserved positioning of proline residues in membrane-spanning helices of ion-channel proteins
    • Woolfson, D. N., S. R. J. Mortishire, and D. H. Williams. 1991. Conserved positioning of proline residues in membrane-spanning helices of ion-channel proteins. Biochem. Biophys. Res. Commun. 175(3):733-737.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , Issue.3 , pp. 733-737
    • Woolfson, D.N.1    Mortishire, S.R.J.2    Williams, D.H.3
  • 37
    • 0025602520 scopus 로고
    • The influence of proline residues on alpha-helical structure
    • Woolfson, D. N., and D. H. Williams. 1990. The influence of proline residues on alpha-helical structure. FEBS Lett. 277:185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 38
    • 0031830342 scopus 로고    scopus 로고
    • Structure of cardiac gap junction intercellular channels
    • Yeager, M. 1998. Structure of cardiac gap junction intercellular channels. J. Struct. Biol. 121:231-245.
    • (1998) J. Struct. Biol. , vol.121 , pp. 231-245
    • Yeager, M.1
  • 39
    • 0025996871 scopus 로고
    • Proline in alpha-helix: Stability and conformation studied by dynamics simulation
    • Yun, R. H., A. Anderson, and J. Hermans. 1991. Proline in alpha-helix: stability and conformation studied by dynamics simulation. Proteins. 10(3):219-228.
    • (1991) Proteins. , vol.10 , Issue.3 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.