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Volumn 130, Issue 1, 2000, Pages 45-53

Polymorphism in the packing of aquaporin-1 tetramers in 2-D crystals

Author keywords

2 dimensional crystal; Aquaporin; Electron crystallography; Membrane protein structure

Indexed keywords

AQUAPORIN; DIOLEOYLPHOSPHATIDYLCHOLINE; LIPID; MAGNESIUM ION; TETRAMER;

EID: 0033911577     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2000.4211     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0029151790 scopus 로고
    • Aquaporin water channels: Unanswered questions and unresolved controversies
    • Agre P., Brown D., Nielsen S. Aquaporin water channels: Unanswered questions and unresolved controversies. Curr. Opin. Cell Biol. 7:1995;472-483.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 472-483
    • Agre, P.1    Brown, D.2    Nielsen, S.3
  • 2
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J., Henderson R. Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy. 14:1984;319-336.
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.1    Henderson, R.2
  • 5
    • 0026969052 scopus 로고
    • Assembly of 2-D membrane protein crystals: Dynamics, crystal order, and fidelity of structure analysis by electron microscopy
    • Engel A., Hoenger A., Hefti A., Henn C., Ford R. C., Kistler J., Zulauf M. Assembly of 2-D membrane protein crystals: Dynamics, crystal order, and fidelity of structure analysis by electron microscopy. J. Struct. Biol. 109:1992;219-234.
    • (1992) J. Struct. Biol. , vol.109 , pp. 219-234
    • Engel, A.1    Hoenger, A.2    Hefti, A.3    Henn, C.4    Ford, R.C.5    Kistler, J.6    Zulauf, M.7
  • 6
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • Gorin M. B., Yancey S. B., Cline J., Revel J. P., Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning. Cell. 39:1984;49-59.
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.P.4    Horwitz, J.5
  • 8
  • 9
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 10
    • 0039507411 scopus 로고
    • Structure of purple membrane from halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5Å resolution
    • Henderson R., Baldwin J. M., Downing K. H., Lepault J., Zemlin F. Structure of purple membrane from halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5Å resolution. Ultramicroscopy. 19:1986;147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 11
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P. N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:1975;28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 12
    • 0031830340 scopus 로고    scopus 로고
    • Progress on structure and function of aquaporin 1
    • Heymann J. B., Agre P., Engel A. Progress on structure and function of aquaporin 1. J. Struct. Biol. 121:1998;191-206.
    • (1998) J. Struct. Biol. , vol.121 , pp. 191-206
    • Heymann, J.B.1    Agre, P.2    Engel, A.3
  • 13
    • 0025087787 scopus 로고
    • Localization of the lipopolysaccharides in metal-shadowed reconstituted lipid-porin membranes
    • Hoenger A., Gross H., Aebi U., Engel A. Localization of the lipopolysaccharides in metal-shadowed reconstituted lipid-porin membranes. J. Struct. Biol. 103:1990;185-195.
    • (1990) J. Struct. Biol. , vol.103 , pp. 185-195
    • Hoenger, A.1    Gross, H.2    Aebi, U.3    Engel, A.4
  • 14
    • 0029647451 scopus 로고
    • Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 A resolution
    • Jap B. K., Li H. Structure of the osmo-regulated H2O-channel, AQP-CHIP, in projection at 3.5 A resolution. J. Mol. Biol. 251:1995;413-420.
    • (1995) J. Mol. Biol. , vol.251 , pp. 413-420
    • Jap, B.K.1    Li, H.2
  • 16
    • 0032500697 scopus 로고    scopus 로고
    • Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
    • Krebs A., Villa C., Edwards P. C., Schertler G. F. Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin. J. Mol. Biol. 282:1998;991-1003.
    • (1998) J. Mol. Biol. , vol.282 , pp. 991-1003
    • Krebs, A.1    Villa, C.2    Edwards, P.C.3    Schertler, G.F.4
  • 17
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D. N., Fujiyoshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature. 367:1994;614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 18
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography [letter] [see comments]
    • Li H., Lee S., Jap B. K. Molecular design of aquaporin-1 water channel as revealed by electron crystallography [letter] [see comments]. Nature Struct. Biol. 4:1997;263-265.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 20
    • 0025727680 scopus 로고
    • Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction
    • Miercke L. J., Betlach M. C., Mitra A. K., Shand R. F., Fong S. K., Stroud R. M. Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction. Biochemistry. 30:1991;3088-3098.
    • (1991) Biochemistry , vol.30 , pp. 3088-3098
    • Miercke, L.J.1    Betlach, M.C.2    Mitra, A.K.3    Shand, R.F.4    Fong, S.K.5    Stroud, R.M.6
  • 21
    • 0028138508 scopus 로고
    • Projection structure of the CHIP28 water channel in lipid bilayer membranes at 12-Å resolution
    • Mitra A. K., Yeager M., van Hoek A., Wiener M. C., Verkman A. S. Projection structure of the CHIP28 water channel in lipid bilayer membranes at 12-Å resolution. Biochemistry. 33:1994;1273S-12740.
    • (1994) Biochemistry , vol.33
    • Mitra, A.K.1    Yeager, M.2    Van Hoek, A.3    Wiener, M.C.4    Verkman, A.S.5
  • 24
    • 20644433762 scopus 로고    scopus 로고
    • Reconstituted aquaporin 1 water channels transport CO2 across membranes
    • Prasad G. V., Coury L. A., Finn F., Zeidel M. L. Reconstituted aquaporin 1 water channels transport CO2 across membranes. J. Biol. Chem. 273:1998;33123-33126.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33123-33126
    • Prasad, G.V.1    Coury, L.A.2    Finn, F.3    Zeidel, M.L.4
  • 25
    • 0027472168 scopus 로고
    • The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel
    • Preston G. M., Jung J. S., Guggino W. B., Agre P. The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J. Biol. Chem. 268:1993;17-20.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17-20
    • Preston, G.M.1    Jung, J.S.2    Guggino, W.B.3    Agre, P.4
  • 27
    • 0025195184 scopus 로고
    • Ca2+, Mg2+, Li+, Na+, and K+ distributions in the headgroup region of binarymembranes of phosphatidylcholine and phosphatidylserine as seen by deuteriumNMR
    • Roux M., Bloom M. Ca2+, Mg2+, Li+, Na+, and K+ distributions in the headgroup region of binarymembranes of phosphatidylcholine and phosphatidylserine as seen by deuteriumNMR. Biochemistry. 29:1990;7077-7089.
    • (1990) Biochemistry , vol.29 , pp. 7077-7089
    • Roux, M.1    Bloom, M.2
  • 29
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G. F., Villa C., Henderson R. Projection structure of rhodopsin. Nature. 362:1993;770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 30
    • 0033617247 scopus 로고    scopus 로고
    • The projection structure of the membrane protein microsomal glutathione transferase at 3A resolution as determined from two-dimensional hexagonal crystals
    • Schmidt-Krey I., Murata K., Hirai T., Mitsuoka K., Cheng Y., Morgenstern R., Fujiyoshi Y., Hebert H. The projection structure of the membrane protein microsomal glutathione transferase at 3A resolution as determined from two-dimensional hexagonal crystals. J. Mol. Biol. 30:1999;243-253.
    • (1999) J. Mol. Biol. , vol.30 , pp. 243-253
    • Schmidt-Krey, I.1    Murata, K.2    Hirai, T.3    Mitsuoka, K.4    Cheng, Y.5    Morgenstern, R.6    Fujiyoshi, Y.7    Hebert, H.8
  • 31
    • 0028914847 scopus 로고
    • Purification and structure-function analysis of native, PNGase F-treated, and endo-β-galactosidase-treated CHIP28 water channels
    • van Hoek A. N., Wiener M. C., Verbavatz J. M., Brown D., Lipniunas P. H., Townsend R. R., Verkman A. S. Purification and structure-function analysis of native, PNGase F-treated, and endo-β-galactosidase-treated CHIP28 water channels. Biochemistry. 34:1995;2212-2219.
    • (1995) Biochemistry , vol.34 , pp. 2212-2219
    • Van Hoek, A.N.1    Wiener, M.C.2    Verbavatz, J.M.3    Brown, D.4    Lipniunas, P.H.5    Townsend, R.R.6    Verkman, A.S.7
  • 32
  • 35
    • 0025091681 scopus 로고
    • Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution
    • Walian P. J., Jap B. K. Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution. J. Mol. Biol. 215:1990;429-438.
    • (1990) J. Mol. Biol. , vol.215 , pp. 429-438
    • Walian, P.J.1    Jap, B.K.2
  • 38
    • 0029375244 scopus 로고
    • Projection map of aquaporin-1 determined by electron crystallography [letter]
    • Walz T., Typke D., Smith B. L., Agre P., Engel A. Projection map of aquaporin-1 determined by electron crystallography [letter]. Nature Struct. Biol. 2:1995;730-732.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 730-732
    • Walz, T.1    Typke, D.2    Smith, B.L.3    Agre, P.4    Engel, A.5
  • 39
    • 0028175266 scopus 로고
    • Biologically active two-dimensional crystals of aquaporin CHIP
    • Walz T., Smith B. L., Zeidel M. L., Engel A., Agre P. Biologically active two-dimensional crystals of aquaporin CHIP. J. Biol. Chem. 269:1994;1583-1586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1583-1586
    • Walz, T.1    Smith, B.L.2    Zeidel, M.L.3    Engel, A.4    Agre, P.5
  • 40
    • 0028314729 scopus 로고
    • Ultrastructure, pharmacologic inhibition, and transport selectivity of aquaporin channel-forming integral protein in proteoliposomes
    • Zeidel M. L., Nielsen S., Smith B. L., Ambudkar S. V., Maunsbach A. B., Agre P. Ultrastructure, pharmacologic inhibition, and transport selectivity of aquaporin channel-forming integral protein in proteoliposomes. Biochemistry. 33:1994;1606-1615.
    • (1994) Biochemistry , vol.33 , pp. 1606-1615
    • Zeidel, M.L.1    Nielsen, S.2    Smith, B.L.3    Ambudkar, S.V.4    Maunsbach, A.B.5    Agre, P.6
  • 41
    • 0024827087 scopus 로고
    • Effect of divalent cations on the structure of dipalmitoylphosphatidylcholine and phosphatidylcholine/phosphatidylglycerol bilayers: An 2H-NMR study
    • Zidovetzki R., Atiya A. W., De Boeck H. Effect of divalent cations on the structure of dipalmitoylphosphatidylcholine and phosphatidylcholine/phosphatidylglycerol bilayers: an 2H-NMR study. Membr. Biochem. 8:1989;177-186.
    • (1989) Membr. Biochem. , vol.8 , pp. 177-186
    • Zidovetzki, R.1    Atiya, A.W.2    De Boeck, H.3


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