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Volumn 490, Issue 7421, 2012, Pages 566-569

Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CAENORHABDITIS ELEGANS PROTEIN; DACTINOMYCIN; MULTIDRUG RESISTANCE PROTEIN; PACLITAXEL;

EID: 84867883248     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11448     Document Type: Article
Times cited : (416)

References (35)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinesehamster ovary cellmutants
    • Juliano, R. L. & Ling, V. A surface glycoprotein modulating drug permeability in Chinesehamster ovary cellmutants. Biochim. Biophys. Acta 455, 152-162 (1976).
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 2
    • 0022923890 scopus 로고
    • The mdr1 gene, responsible for multidrug-resistance, codes for P-glycoprotein
    • Ueda, K. et al. The mdr1 gene, responsible for multidrug-resistance, codes for P-glycoprotein. Biochem. Biophys. Res. Commun. 141, 956-962 (1986).
    • (1986) Biochem. Biophys. Res. Commun , vol.141 , pp. 956-962
    • Ueda, K.1
  • 3
    • 84856271899 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter
    • Sharom, F. J. The P-glycoprotein multidrug transporter. Essays Biochem. 50, 161-178 (2011).
    • (2011) Essays Biochem , vol.50 , pp. 161-178
    • Sharom, F.J.1
  • 4
    • 0026580336 scopus 로고
    • Is the multidrug transporter a flippase?
    • Higgins, C. F. & Gottesman, M. M. Is the multidrug transporter a flippase? Trends Biochem. Sci. 17, 18-21 (1992).
    • (1992) Trends Biochem. Sci , vol.17 , pp. 18-21
    • Higgins, C.F.1    Gottesman, M.M.2
  • 5
    • 57049124822 scopus 로고    scopus 로고
    • Structural insights into ABC transporter mechanism
    • Oldham, M. L., Davidson, A. L. & Chen, J. Structural insights into ABC transporter mechanism. Curr. Opin. Struct. Biol. 18, 726-733 (2008).
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 726-733
    • Oldham, M.L.1    Davidson, A.L.2    Chen, J.3
  • 6
    • 2442597224 scopus 로고    scopus 로고
    • Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein. J. Biol. Chem. 279, 18232-18238 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 18232-18238
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 7
    • 1542320036 scopus 로고    scopus 로고
    • Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of humanP-glycoprotein are close together on the cytoplasmic side of the membrane
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of humanP-glycoprotein are close together on the cytoplasmic side of the membrane. J. Biol. Chem. 279, 7692-7697 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 7692-7697
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 8
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket. Biochem. J. 396, 537-545 (2006).
    • (2006) Biochem. J , vol.396 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 9
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket. Biochem. J. 399, 351-359 (2006).
    • (2006) Biochem. J , vol.399 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 10
    • 36148958644 scopus 로고    scopus 로고
    • Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites. J. Biol. Chem. 282, 32043-32052 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 32043-32052
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 11
    • 14644425991 scopus 로고    scopus 로고
    • Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?
    • Loo, T. W. & Clarke, D. M. Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"? Biochem. Biophys. Res. Commun. 329, 419-422 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 419-422
    • Loo, T.W.1    Clarke, D.M.2
  • 12
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks, J. K., Wooding, C. & Linton, K. J. Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein. FASEB J. 21, 3937-3948 (2007).
    • (2007) FASEB J , vol.21 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 13
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo, T. W. & Clarke, D. M. Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein. J. Biol. Chem. 268, 19965-19972 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 19965-19972
    • Loo, T.W.1    Clarke, D.M.2
  • 14
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • Loo, T. W. & Clarke, D. M. Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities. J. Biol. Chem. 270, 21449-21452 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 15
    • 0024307162 scopus 로고
    • Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance
    • Azzaria, M., Schurr, E. & Gros, P. Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance. Mol. Cell. Biol. 9, 5289-5297 (1989).
    • (1989) Mol. Cell. Biol , vol.9 , pp. 5289-5297
    • Azzaria, M.1    Schurr, E.2    Gros, P.3
  • 16
    • 0023840065 scopus 로고
    • Purification of the 170-to 180-kilodalton membrane glycoprotein associated with multidrug resistance. 170-to 180-kilodalton membrane glycoprotein is an ATPase
    • Hamada, H. & Tsuruo, T. Purification of the 170-to 180-kilodalton membrane glycoprotein associated with multidrug resistance. 170-to 180-kilodalton membrane glycoprotein is an ATPase. J. Biol. Chem. 263, 1454-1458 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 1454-1458
    • Hamada, H.1    Tsuruo, T.2
  • 17
    • 0027417398 scopus 로고
    • Characterization of the adenosine triphosphatase activity ofChinesehamster P-glycoprotein
    • Al-Shawi, M. K. & Senior, A. E. Characterization of the adenosine triphosphatase activity ofChinesehamster P-glycoprotein. J. Biol. Chem. 268, 4197-4206 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 4197-4206
    • Al-Shawi, M.K.1    Senior, A.E.2
  • 18
    • 0032321894 scopus 로고    scopus 로고
    • Drug-stimulatable ATPase activity in crudemembranes of human MDR1-transfected mammalian cells
    • Ambudkar, S. V. Drug-stimulatable ATPase activity in crudemembranes of human MDR1-transfected mammalian cells. Methods Enzymol. 292, 504-514 (1998).
    • (1998) Methods Enzymol , vol.292 , pp. 504-514
    • Ambudkar, S.V.1
  • 19
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi, B., Price, E. M., Boucher, R. C., Germann, U. A. & Scarborough, G. A. Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J. Biol. Chem. 267, 4854-4858 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 4854-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 20
    • 0346732289 scopus 로고    scopus 로고
    • Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein
    • Al-Shawi, M. K., Polar, M. K.,Omote, H. & Figler, R. A. Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein. J. Biol. Chem. 278, 52629-52640 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 52629-52640
    • Al-Shawi, M.K.1    Polar, M.K.2    Omote, H.3    Figler, R.A.4
  • 21
    • 0030791978 scopus 로고    scopus 로고
    • Structure-activity relationships of P-glycoprotein interacting drugs: Kinetic characterization of their effects on ATPase activity
    • Litman, T., Zeuthen, T., Skovsgaard, T.&Stein, W. D. Structure-activity relationships of P-glycoprotein interacting drugs: kinetic characterization of their effects on ATPase activity. Biochim. Biophys. Acta 1361, 159-168 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 159-168
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 22
    • 42449161053 scopus 로고    scopus 로고
    • Relationship between drugs and functional activity of various mammalian P-glycoproteins (ABCB1)
    • Ambudkar, S. V., Kim, I.-W. & Booth-Genthe, C. Relationship between drugs and functional activity of various mammalian P-glycoproteins (ABCB1). Mini Rev. Med. Chem. 8, 193-200 (2008).
    • (2008) Mini Rev. Med. Chem , vol.8 , pp. 193-200
    • Ambudkar, S.V.1    Kim, I.-W.2    Booth-Genthe, C.3
  • 23
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for polyspecific drug binding
    • Aller, S. G. et al. Structure of P-glycoprotein reveals a molecular basis for polyspecific drug binding. Science 323, 1718-1722 (2009).
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1
  • 24
    • 33644672481 scopus 로고    scopus 로고
    • Quantification and characterization of P-glycoprotein-substrate interactions
    • Gatlik-Landwojtowicz, E., Aanismaa, P. & Seelig, A. Quantification and characterization of P-glycoprotein-substrate interactions. Biochemistry 45, 3020-3032 (2006).
    • (2006) Biochemistry , vol.45 , pp. 3020-3032
    • Gatlik-Landwojtowicz, E.1    Aanismaa, P.2    Seelig, A.3
  • 25
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in theABC transporter MsbA: Alternating access with a twist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B.& Chang, G. Flexibility in theABC transporter MsbA: alternating access with a twist. Proc.Natl Acad. Sci.USA104, 19005-19010 (2007).
    • (2007) Proc.Natl Acad. Sci.USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 26
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti, E. & Hunte, C. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159, 261-267 (2007).
    • (2007) J. Struct. Biol , vol.159 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 27
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare, D., Oldham, M. L., Orelle, C., Davidson, A. L. & Chen, J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 33, 528-536 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 28
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., Hofnung, M. & Dassa, E. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16, 3066-3077 (1997).
    • (1997) EMBO J , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 29
    • 57649134969 scopus 로고    scopus 로고
    • Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR). J. Biol. Chem. 283, 28190-28197 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 28190-28197
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 30
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
    • Loo, T. W., Bartlett, M. C. & Clarke, D. M. Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis. J. Biol. Chem. 284, 24074-24087 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 31
    • 0027484689 scopus 로고
    • Absence of cooperativity for MgATPand verapamil effects on the ATPase activity of P-glycoprotein containing membrane vesicles
    • Garrigos, M., Belehradek, J. Jr, Mir, L. M.&Orlowski, S.Absence of cooperativity for MgATPand verapamil effects on the ATPase activity of P-glycoprotein containing membrane vesicles. Biochem. Biophys. Res. Commun. 196, 1034-1041 (1993).
    • (1993) Biochem. Biophys. Res. Commun , vol.196 , pp. 1034-1041
    • Garrigos, M.1    Belehradek Jr., J.2    Mir, L.M.3    Orlowski, S.4
  • 32
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A. T. Version 1.2 of the crystallography and NMR system. Nature Protocols 2, 2728-2733 (2007).
    • (2007) Nature Protocols , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3


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