메뉴 건너뛰기




Volumn 38, Issue 2, 2005, Pages 117-126

Structure, orientation, and conformational changes in transmembrane domains of multidrug transporters

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN P; LIGAND; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN 1;

EID: 13844322130     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar040021o     Document Type: Article
Times cited : (7)

References (37)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano, R. L.; Ling, V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta 1976, 455, 152-162.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 2
    • 0442307441 scopus 로고    scopus 로고
    • Efflux-mediated drug resistance in bacteria
    • Li, X. Z.; Nikaido, H. Efflux-mediated drug resistance in bacteria. Drugs 2004, 64, 159-204.
    • (2004) Drugs , vol.64 , pp. 159-204
    • Li, X.Z.1    Nikaido, H.2
  • 3
    • 0028822932 scopus 로고
    • New mechanisms of drug resistance in parasitic protozoa
    • Borst, P.; Ouellette, M. New mechanisms of drug resistance in parasitic protozoa. Annu. Rev. Microbiol. 1995, 49, 427-460.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 427-460
    • Borst, P.1    Ouellette, M.2
  • 4
    • 0041833334 scopus 로고    scopus 로고
    • ABC-transporters: Implications on drug resistance from microorganisms to human cancers
    • Lage, H. ABC-transporters: Implications on drug resistance from microorganisms to human cancers. Int. J. Antimicrob. Agents 2003, 22, 188-199.
    • (2003) Int. J. Antimicrob. Agents , vol.22 , pp. 188-199
    • Lage, H.1
  • 6
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistance
    • Endicott, J. A.; Ling, V. The biochemistry of P-glycoprotein-mediated multidrug resistance. Annu. Rev. Biochem. 1989, 58, 137-171.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 137-171
    • Endicott, J.A.1    Ling, V.2
  • 8
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene
    • van Veen, H. W.; Callaghan, R.; Soceneantu, L.; Sardini, A.; Konings, W. N.; Higgins, C. F. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature 1998, 391, 291-295.
    • (1998) Nature , vol.391 , pp. 291-295
    • Van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 9
    • 0033609856 scopus 로고    scopus 로고
    • The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface
    • Loo, T. W.; Clarke, D. M. The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface. J. Biol. Chem. 1999, 274, 24759-24765.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 10
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactococcus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • Bolhuis, H.; van Veen, H. W.; Molenaar, D.; Poolman, B.; Driessen, A. J.; Konings, W. N. Multidrug resistance in Lactococcus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J. 1996, 15, 4239-4245.
    • (1996) EMBO J. , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    Van Veen, H.W.2    Molenaar, D.3    Poolman, B.4    Driessen, A.J.5    Konings, W.N.6
  • 11
    • 0035853848 scopus 로고    scopus 로고
    • Major photoaffinity drug binding sites in multidrug resistance protein 1 (MRP1) are within transmembrane domains 10-11 and 16-17
    • Daoud, R.; Julien, M.; Gros, P.; Georges, E. Major photoaffinity drug binding sites in multidrug resistance protein 1 (MRP1) are within transmembrane domains 10-11 and 16-17. J. Biol. Chem. 2001, 276, 12324-12330.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12324-12330
    • Daoud, R.1    Julien, M.2    Gros, P.3    Georges, E.4
  • 12
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G.; Roth, C. B. Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 2001, 293, 1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 13
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P.; Lee, A. T.; Rees, D. C. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 2002, 296, 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 14
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami, S.; Nakashima, R.; Yamashita, E.; Yamaguchi, A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 2002, 419, 587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 15
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • Margolles, A.; Putman, M.; van Veen, H. W.; Konings, W. N. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry 1999, 38, 16298-16306.
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 17
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh, E.; Raussens, V.; Ruysschaert, J. M. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1999, 1422, 105-185.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 18
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated films
    • Goormaghtigh, E.; Cabiaux, V.; Ruysschaert, J. M. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 1990, 193, 409-420.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 19
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 20
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectrs
    • Byler, D. M.; Susi, H. Examination of the secondary structure of proteins by deconvolved FTIR spectrs. Biopolymers 1986, 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 21
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis
    • Vigano, C.; Margolles, A.; van Veen, H. W.; Konings, W. N.; Ruysschaert, J. M. Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis. J. Biol. Chem. 2000, 275, 10962-10967.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10962-10967
    • Vigano, C.1    Margolles, A.2    Van Veen, H.W.3    Konings, W.N.4    Ruysschaert, J.M.5
  • 23
    • 0035797927 scopus 로고    scopus 로고
    • Structure and dynamics of the membrane-embedded domain of LmrA investigated by coupling polarized ATR-FTIR spectroscopy and (1)H/(2)H exchange
    • Grimard, V.; Vigano, C.; Margolles, A.; Wattiez, R.; van Veen, H. W.; Konings, W. N.; Ruysschaert, J. M.; Goormaghtigh, E. Structure and dynamics of the membrane-embedded domain of LmrA investigated by coupling polarized ATR-FTIR spectroscopy and (1)H/(2)H exchange. Biochemistry 2001, 40, 11876-11886.
    • (2001) Biochemistry , vol.40 , pp. 11876-11886
    • Grimard, V.1    Vigano, C.2    Margolles, A.3    Wattiez, R.4    Van Veen, H.W.5    Konings, W.N.6    Ruysschaert, J.M.7    Goormaghtigh, E.8
  • 24
    • 0029784872 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis
    • Sonveaux, N.; Shapiro, A. B.; Goormaghtigh, E.; Ling, V.; Ruysschaert, J. M. Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis. J. Biol. Chem. 1996, 271, 24617-24624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3    Ling, V.4    Ruysschaert, J.M.5
  • 25
    • 0037085284 scopus 로고    scopus 로고
    • Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy
    • Vigano, C.; Julien, M.; Carrier, I.; Gros, P.; Ruysschaert, J. M. Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy. J. Biol. Chem. 2002, 277, 5008-5016.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5008-5016
    • Vigano, C.1    Julien, M.2    Carrier, I.3    Gros, P.4    Ruysschaert, J.M.5
  • 26
    • 0034459184 scopus 로고    scopus 로고
    • Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation, and tertiary structure changes in peptides and membrane proteins
    • Vigano, C.; Manciu, L.; Buyse, F.; Goormaghtigh, E.; Ruysschaert, J. M. Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation, and tertiary structure changes in peptides and membrane proteins. Biopolymers 2000, 55, 373-380.
    • (2000) Biopolymers , vol.55 , pp. 373-380
    • Vigano, C.1    Manciu, L.2    Buyse, F.3    Goormaghtigh, E.4    Ruysschaert, J.M.5
  • 27
    • 0034711094 scopus 로고    scopus 로고
    • Multidrug resistance protein MRP1 reconstituted into lipid vesicles: Secondary structure and nucleotide-induced tertiary structure changes
    • Manciu, L.; Chang, X. B.; Riordan, J. R.; Ruysschaert, J. M. Multidrug resistance protein MRP1 reconstituted into lipid vesicles: Secondary structure and nucleotide-induced tertiary structure changes. Biochemistry 2000, 39, 13026-13033.
    • (2000) Biochemistry , vol.39 , pp. 13026-13033
    • Manciu, L.1    Chang, X.B.2    Riordan, J.R.3    Ruysschaert, J.M.4
  • 28
  • 29
    • 0037163877 scopus 로고    scopus 로고
    • A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter
    • Vigano, C.; Grimard, V.; Margolles, A.; Goormaghtigh, E.; van Veen, H. W.; Konings, W. N.; Ruysschaert, J. M. A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter. FEBS Lett. 2002, 530, 197-203.
    • (2002) FEBS Lett. , vol.530 , pp. 197-203
    • Vigano, C.1    Grimard, V.2    Margolles, A.3    Goormaghtigh, E.4    Van Veen, H.W.5    Konings, W.N.6    Ruysschaert, J.M.7
  • 30
    • 0033580854 scopus 로고    scopus 로고
    • Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis
    • Sonveaux, N.; Vigano, C.; Shapiro, A. B.; Ling, V.; Ruysschaert, J. M. Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis. J. Biol. Chem. 1999, 274, 17649-17654.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17649-17654
    • Sonveaux, N.1    Vigano, C.2    Shapiro, A.B.3    Ling, V.4    Ruysschaert, J.M.5
  • 31
    • 0035937483 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in the human multidrug resistance protein MRP1 are related to the capacity of chemotherapeutic drugs to accumulate or not in resistant cells
    • Manciu, L.; Chang, X.; Riordan, J. R.; Buyse, F.; Ruysschaert, J. M. Nucleotide-induced conformational changes in the human multidrug resistance protein MRP1 are related to the capacity of chemotherapeutic drugs to accumulate or not in resistant cells. FEBS Lett. 2001, 493, 31-35.
    • (2001) FEBS Lett. , vol.493 , pp. 31-35
    • Manciu, L.1    Chang, X.2    Riordan, J.R.3    Buyse, F.4    Ruysschaert, J.M.5
  • 33
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • Chang, X. B.; Hou, Y. X.; Riordan, J. R. ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 1997, 272, 30962-30968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 34
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon, A. I.; Soekarjo, M. W.; De Gier, J.; De Kruijff, B. The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 1990, 29, 8229-8240
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 35
    • 0022424046 scopus 로고
    • Depth-dependent fluorescent quenching in micelles and membranes
    • Blatt, E.; Sawyer, W. H. Depth-dependent fluorescent quenching in micelles and membranes. Biochim. Biophys. Acta 1985, 822, 43-62.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 43-62
    • Blatt, E.1    Sawyer, W.H.2
  • 36
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J.; Holloway, P. W. Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry 1987, 26, 1783-1788.
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.