메뉴 건너뛰기




Volumn 85, Issue 5, 2003, Pages 3097-3105

Effect of Detergents on the Association of the Glycophorin A Transmembrane Helix

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; DIMER; GLYCOPHORIN A; PEPTIDE HORMONE;

EID: 0242353821     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74728-6     Document Type: Article
Times cited : (113)

References (45)
  • 1
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics versus environment: Simulations of OmpA in a micelle and in a bilayer
    • Bond, P. J., and M. S. P. Sansom. 2003. Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer. J. Mol. Biol. 329:1035-1053.
    • (2003) J. Mol. Biol. , vol.329 , pp. 1035-1053
    • Bond, P.J.1    Sansom, M.S.P.2
  • 3
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann, B. J., W. J. Knowles, and V. T. Marchesi. 1989. Synthetic peptides mimic the assembly of transmembrane glycoproteins. J. Biol. Chem. 264:4033-4037.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4033-4037
    • Bormann, B.J.1    Knowles, W.J.2    Marchesi, V.T.3
  • 4
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • Brosig, B., and D. Langosch. 1998. The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues. Protein Sci. 7:1052-1056.
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 5
    • 0032805390 scopus 로고    scopus 로고
    • A method for determining transmembrane helix association and orientation in detergent micelles using small angle x-ray scattering
    • Bu, Z., and D. M. Engelman. 1999. A method for determining transmembrane helix association and orientation in detergent micelles using small angle x-ray scattering. Biophys. J. 77:1064-1073.
    • (1999) Biophys. J. , vol.77 , pp. 1064-1073
    • Bu, Z.1    Engelman, D.M.2
  • 6
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., and C. B. Roth. 2001. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science. 293:1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 7
    • 0030156640 scopus 로고    scopus 로고
    • Aqueous solutions of zwitterionic surfactants with varying carbon number of the intercharge group. 3. Intermicellar interactions
    • Chevalier, Y., N. Kamenka, M. Chorro, and R. Zana. 1996. Aqueous solutions of zwitterionic surfactants with varying carbon number of the intercharge group. 3. intermicellar interactions. Langmuir. 12:3225-3232.
    • (1996) Langmuir , vol.12 , pp. 3225-3232
    • Chevalier, Y.1    Kamenka, N.2    Chorro, M.3    Zana, R.4
  • 8
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson, J. P., J. S. Weinger, and D. M. Engelman. 2002. Motifs of serine and threonine can drive association of transmembrane helices. J. Mol. Biol. 316:799-805.
    • (2002) J. Mol. Biol. , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 9
    • 0037008040 scopus 로고    scopus 로고
    • The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane alpha-helical peptides depend on the nature of interfacially exposed aromatic and charged residues
    • de Planque, M. R., J. W. Boots, D. T. Rijkers, R. M. Liskamp, D. V. Greathouse, and J. A. Killian. 2002. The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane alpha-helical peptides depend on the nature of interfacially exposed aromatic and charged residues. Biochemistry. 41:8396-8404.
    • (2002) Biochemistry , vol.41 , pp. 8396-8404
    • De Planque, M.R.1    Boots, J.W.2    Rijkers, D.T.3    Liskamp, R.M.4    Greathouse, D.V.5    Killian, J.A.6
  • 10
    • 0019604334 scopus 로고
    • A fluorimetric method for the estimation of the critical micelle concentration of surfactants
    • De Vendittis, E., G. Palumbo, G. Parlato, and V. Bocchini. 1981. A fluorimetric method for the estimation of the critical micelle concentration of surfactants. Anal. Biochem. 115:278-286.
    • (1981) Anal. Biochem. , vol.115 , pp. 278-286
    • De Vendittis, E.1    Palumbo, G.2    Parlato, G.3    Bocchini, V.4
  • 12
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham, S., and J. U. Bowie. 2002. Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316:1-6.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 13
    • 0035369984 scopus 로고    scopus 로고
    • High-yield synthesis and purification of an α-helical transmembrane domain
    • Fisher, L. E., and D. M. Engelman. 2001. High-yield synthesis and purification of an α-helical transmembrane domain. Anal. Biochem. 293:102-108.
    • (2001) Anal. Biochem. , vol.293 , pp. 102-108
    • Fisher, L.E.1    Engelman, D.M.2
  • 14
    • 0032732426 scopus 로고    scopus 로고
    • Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain
    • Fisher, L. E., D. M. Engelman, and J. N. Sturgis. 1999. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain. J. Mol. Biol. 293:639-651.
    • (1999) J. Mol. Biol. , vol.293 , pp. 639-651
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 15
    • 0036408542 scopus 로고    scopus 로고
    • Standardizing the free-energy change of Helix-helix interactions
    • Fleming, K. G. 2002. Standardizing the free-energy change of Helix-helix interactions. J. Mol. Biol. 323:563-571.
    • (2002) J. Mol. Biol. , vol.323 , pp. 563-571
    • Fleming, K.G.1
  • 16
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane alpha-helix dimerization
    • Fleming, K. G., A. L. Ackerman, and D. M. Engelman. 1997. The effect of point mutations on the free energy of transmembrane alpha-helix dimerization. J. Mol. Biol. 272:266-275.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 17
    • 0035807810 scopus 로고    scopus 로고
    • Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants
    • Fleming, K. G., and D. M. Engelman. 2001. Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proc. Natl. Acad. Sci. USA. 98:14340-14344.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14340-14344
    • Fleming, K.G.1    Engelman, D.M.2
  • 19
    • 0036008218 scopus 로고    scopus 로고
    • Position of residues in transmembrane peptides with respect to the lipid bilayer: A combined lipid Noes and water chemical exchange approach in phospholipid bicelles
    • Glover, K. J., J. A. Whiles, R. R. Vold, and G. Melacini. 2002. Position of residues in transmembrane peptides with respect to the lipid bilayer: a combined lipid Noes and water chemical exchange approach in phospholipid bicelles. J. Biomol. NMR. 22:57-64.
    • (2002) J. Biomol. NMR , vol.22 , pp. 57-64
    • Glover, K.J.1    Whiles, J.A.2    Vold, R.R.3    Melacini, G.4
  • 20
  • 22
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and G. von Heijne. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 23
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D., B. Brosig, H. Kolmar, and H. J. Fritz. 1996. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263:525-530.
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 25
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane of α-helices
    • Lemmon, M. A., J. M. Flanagan, H. R. Treutlein, J. Zhang, and D. M. Engelman. 1992b. Sequence specificity in the dimerization of transmembrane of α-helices. Biochemistry. 31:12719-12725.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 26
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., A. T. Lee, and D. C. Rees. 2002. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science. 296:1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 28
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science. 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 30
    • 0031551579 scopus 로고    scopus 로고
    • Helix-helix packing in a membrane-like environment
    • Mingarro, I., A. Elofsson, and G. von Heijne. 1997. Helix-helix packing in a membrane-like environment. J. Mol. Biol. 272:633-641.
    • (1997) J. Mol. Biol. , vol.272 , pp. 633-641
    • Mingarro, I.1    Elofsson, A.2    Von Heijne, G.3
  • 31
    • 0029893893 scopus 로고    scopus 로고
    • Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: A rapid way to map helix-helix interactions in integral membrane proteins
    • Mingarro, I., P. Whitley, M. A. Lemmon, and G. von Heijne. 1996. Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: a rapid way to map helix-helix interactions in integral membrane proteins. Protein Sci. 5:1339-1341.
    • (1996) Protein Sci. , vol.5 , pp. 1339-1341
    • Mingarro, I.1    Whitley, P.2    Lemmon, M.A.3    Von Heijne, G.4
  • 33
    • 0343962575 scopus 로고    scopus 로고
    • Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process
    • Orzaez, M., E. Perez-Paya, and I. Mingarro. 2000. Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process. Protein Sci. 9:1246-1253.
    • (2000) Protein Sci. , vol.9 , pp. 1246-1253
    • Orzaez, M.1    Perez-Paya, E.2    Mingarro, I.3
  • 34
    • 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. 277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 35
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane protein folding and oligomerization: the two-stage model. Biochemistry. 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 36
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 37
    • 1842650004 scopus 로고
    • Growth of sodium dodecyl sulfate micelles with detergent concentration
    • Quina, F. H., P. M. Nassar, J. B. S. Bonilha, and B. L. Bales. 1995. Growth of sodium dodecyl sulfate micelles with detergent concentration. J. Phys. Chem. 99:17028-17031.
    • (1995) J. Phys. Chem. , vol.99 , pp. 17028-17031
    • Quina, F.H.1    Nassar, P.M.2    Bonilha, J.B.S.3    Bales, B.L.4
  • 38
    • 0035783023 scopus 로고    scopus 로고
    • Stability of membrane proteins: Relevance for the selection of appropriate methods for high-resolution structure determinations
    • Rosenbusch, J. P. 2001. Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations. J. Struct. Biol. 136:144-157.
    • (2001) J. Struct. Biol. , vol.136 , pp. 144-157
    • Rosenbusch, J.P.1
  • 39
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ, W. P., and D. M. Engelman. 1999. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. USA. 96:863-868.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 40
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions
    • Senes, A., M. Gerstein, and D. M. Engelman. 2000. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions. J. Mol. Biol. 296:921-936.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 41
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui, H., B. G. Han, J. K. Lee, P. Walian, and B. K. Jap, 2001. Structural basis of water-specific transport through the AQP1 water channel. Nature. 414:872-878.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 43
    • 0027092981 scopus 로고
    • The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices
    • Treutlein, H. R., M. A. Lemmon, D. M. Engelman, and A. T. Brunger. 1992. The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices. Biochemistry. 31:12726-12732.
    • (1992) Biochemistry , vol.31 , pp. 12726-12732
    • Treutlein, H.R.1    Lemmon, M.A.2    Engelman, D.M.3    Brunger, A.T.4
  • 45
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J. 1964. Linked functions and reciprocal effects in hemoglobin: a second look, Adv. Protein Chem. 19:223-286.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • Wyman, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.