메뉴 건너뛰기




Volumn 51, Issue 25, 2012, Pages 5125-5141

Catalytic transitions in the human mdr1 P-glycoprotein drug binding sites

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; ATP-BINDING CASSETTE; CATALYTIC MECHANISMS; DRUG BINDING; DYNAMICS SIMULATION; EXTRACELLULAR; EXTRACELLULAR SPACE; MULTIDRUG RESISTANCE; NUCLEOTIDE-BINDING DOMAIN; P-GLYCOPROTEIN; PROTEIN STRUCTURES; STRUCTURE ANALYSIS; TARGETED MOLECULAR DYNAMICS; TRANS-MEMBRANE DOMAINS; TRANSITION STATE;

EID: 84862890003     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300299z     Document Type: Article
Times cited : (75)

References (86)
  • 1
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • DOI 10.1006/jmbi.1999.2993
    • Holland, I. B. and Blight, M. A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans J. Mol. Biol. 293, 381-399 (Pubitemid 29516178)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 381-399
    • Holland, I.B.1    A. Blight, M.2
  • 2
    • 0032226550 scopus 로고    scopus 로고
    • Structure and function of multidrug transporters
    • van Veen, H. W. and Konings, W. N. (1998) Structure and function of multidrug transporters Adv. Exp. Med. Biol. 456, 145-158
    • (1998) Adv. Exp. Med. Biol. , vol.456 , pp. 145-158
    • Van Veen, H.W.1    Konings, W.N.2
  • 3
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: How P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • DOI 10.1158/1535-7163.MCT-06-0155
    • Sauna, Z. E. and Ambudkar, S. V. (2007) About a switch: How P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work Mol. Cancer Ther. 6, 13-23 (Pubitemid 46206664)
    • (2007) Molecular Cancer Therapeutics , vol.6 , Issue.1 , pp. 13-23
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 5
    • 38349136208 scopus 로고    scopus 로고
    • Genomics and the mechanism of P-glycoprotein (ABCB1)
    • Sauna, Z. E., Kim, I., and Ambudkar, S. V. (2007) Genomics and the mechanism of P-glycoprotein (ABCB1) J. Bioenerg. Biomembr. 39, 481-487
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 481-487
    • Sauna, Z.E.1    Kim, I.2    Ambudkar, S.V.3
  • 6
    • 0026669363 scopus 로고
    • Characterization of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann, E. P., Currier, S. J., Gottesman, M. M., and Pastan, I. (1992) Characterization of the azidopine and vinblastine binding site of P-glycoprotein J. Biol. Chem. 267, 21020-21026
    • (1992) J. Biol. Chem. , vol.267 , pp. 21020-21026
    • Bruggemann, E.P.1    Currier, S.J.2    Gottesman, M.M.3    Pastan, I.4
  • 7
    • 0032559001 scopus 로고    scopus 로고
    • Identification of the cyclosporin-binding site in P-glycoprotein
    • DOI 10.1021/bi981992c
    • Demeule, M., Laplante, A., Murphy, G. F., Wenger, R. M., and Béliveau, R. (1998) Identification of the cyclosporin-binding site in P-glycoprotein Biochemistry 37, 18110-18118 (Pubitemid 29023968)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 18110-18118
    • Demeule, M.1    Laplante, A.2    Murphy, G.F.3    Wenger, R.M.4    Beliveau, R.5
  • 8
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • DOI 10.1074/jbc.M208433200
    • Loo, T. W. and Clarke, D. M. (2002) Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein J. Biol. Chem. 277, 44332-44338 (Pubitemid 36157868)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 9
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • DOI 10.1042/BJ20060715
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2006) Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket Biochem. J. 399, 351-359 (Pubitemid 44570297)
    • (2006) Biochemical Journal , vol.399 , Issue.2 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 10
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • DOI 10.1042/BJ20060012
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2006) Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket Biochem. J. 396, 537-545 (Pubitemid 44228168)
    • (2006) Biochemical Journal , vol.396 , Issue.3 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 11
    • 0028901538 scopus 로고
    • Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by mdr1
    • Zhang, X., Collins, K. I., and Greenberger, L. M. (1995) Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by mdr1 J. Biol. Chem. 270, 5441-5448
    • (1995) J. Biol. Chem. , vol.270 , pp. 5441-5448
    • Zhang, X.1    Collins, K.I.2    Greenberger, L.M.3
  • 12
    • 0141994817 scopus 로고    scopus 로고
    • Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein
    • DOI 10.1074/jbc.M308559200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein J. Biol. Chem. 278, 39706-39710 (Pubitemid 37248532)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39706-39710
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 13
    • 0029559159 scopus 로고
    • The catalytic cycle of P-glycoprotein
    • DOI 10.1016/0014-5793(95)01345-8
    • Senior, A. E., al-Shawi, M. K., and Urbatsch, I. L. (1995) The catalytic cycle of P-glycoprotein FEBS Lett. 377, 285-289 (Pubitemid 26025714)
    • (1995) FEBS Letters , vol.377 , Issue.3 , pp. 285-289
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3
  • 14
    • 0028940488 scopus 로고
    • ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells
    • Senior, A. E., al-Shawi, M. K., and Urbatsch, I. L. (1995) ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells J. Bioenerg. Biomembr. 27, 31-36
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 31-36
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3
  • 15
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P- glycoprotein
    • DOI 10.1021/bi00189a008
    • Urbatsch, I. L., al-Shawi, M. K., and Senior, A. E. (1994) Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein Biochemistry 33, 7069-7076 (Pubitemid 24208742)
    • (1994) Biochemistry , vol.33 , Issue.23 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 16
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch, I. L., Sankaran, B., Bhagat, S., and Senior, A. E. (1995) Both P-glycoprotein nucleotide-binding sites are catalytically active J. Biol. Chem. 270, 26956-26961
    • (1995) J. Biol. Chem. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 17
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller, S. G., Yu, J., Ward, A., Weng, Y., and Chittaboina, S. 2009, Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding Science 323, 1718-1722
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5
  • 18
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • DOI 10.1038/nature05155, PII NATURE05155
    • Dawson, R. J. P. and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter Nature 443, 180-185 (Pubitemid 44387602)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 19
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • DOI 10.1016/j.febslet.2007.01.073, PII S0014579307001226
    • Dawson, R. J. P. and Locher, K. P. (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP FEBS Lett. 581, 935-938 (Pubitemid 46282725)
    • (2007) FEBS Letters , vol.581 , Issue.5 , pp. 935-938
    • Dawson, R.J.P.1    Locher, K.P.2
  • 20
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MSBA: Alternating access with a twist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B., and Chang, G. (2007) Flexibility in the ABC transporter MSBA: Alternating access with a twist Proc. Natl. Acad. Sci. U.S.A. 104, 19005-19010
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 21
    • 80053074680 scopus 로고    scopus 로고
    • Reaction chemistry ABC-style
    • Senior, A. E. (2011) Reaction chemistry ABC-style Proc. Natl. Acad. Sci. U.S.A. 108, 15015-15016
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15015-15016
    • Senior, A.E.1
  • 22
    • 50849114847 scopus 로고    scopus 로고
    • Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus
    • Velamakanni, S., Yao, Y., Gutmann, D. A. P., and van Veen, H. W. (2008) Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus Biochemistry 47, 9300-9308
    • (2008) Biochemistry , vol.47 , pp. 9300-9308
    • Velamakanni, S.1    Yao, Y.2    Gutmann, D.A.P.3    Van Veen, H.W.4
  • 23
    • 50249114683 scopus 로고    scopus 로고
    • An improved relaxed complex scheme for receptor flexibility in computer-aided drug design
    • Amaro, R. E., Baron, R., and McCammon, J. A. (2008) An improved relaxed complex scheme for receptor flexibility in computer-aided drug design J. Comput.-Aided Mol. Des. 22, 693-705
    • (2008) J. Comput.-Aided Mol. Des. , vol.22 , pp. 693-705
    • Amaro, R.E.1    Baron, R.2    McCammon, J.A.3
  • 24
    • 79960313955 scopus 로고    scopus 로고
    • Molecular recognition in the case of flexible targets
    • Ivetac, A. and McCammon, J. A. (2011) Molecular recognition in the case of flexible targets Curr. Pharm. Des. 17, 1663-1671
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 1663-1671
    • Ivetac, A.1    McCammon, J.A.2
  • 25
    • 0037157153 scopus 로고    scopus 로고
    • Computational drug design accommodating receptor flexibility: The relaxed complex scheme
    • DOI 10.1021/ja0260162
    • Lin, J., Perryman, A. L., Schames, J. R., and McCammon, J. A. (2002) Computational drug design accommodating receptor flexibility: The relaxed complex scheme J. Am. Chem. Soc. 124, 5632-5633 (Pubitemid 34533490)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.20 , pp. 5632-5633
    • Lin, J.-H.1    Perryman, A.L.2    Schames, J.R.3    McCammon, J.A.4
  • 26
    • 33749442647 scopus 로고    scopus 로고
    • Multiseq: Unifying sequence and structure data for evolutionary analysis
    • Roberts, E., Eargle, J., Wright, D., and Luthey-Schulten, Z. (2006) Multiseq: Unifying sequence and structure data for evolutionary analysis BMC Bioinf. 7, 382
    • (2006) BMC Bioinf. , vol.7 , pp. 382
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 27
    • 0026614434 scopus 로고
    • The T R structural transition of insulin; Pathways suggested by targeted energy minimization
    • Engels, M., Jacoby, E., Krüger, P., Schlitter, J., and Wollmer, A. (1992) The T R structural transition of insulin; pathways suggested by targeted energy minimization Protein Eng. 5, 669-677
    • (1992) Protein Eng. , vol.5 , pp. 669-677
    • Engels, M.1    Jacoby, E.2    Krüger, P.3    Schlitter, J.4    Wollmer, A.5
  • 28
    • 0028455053 scopus 로고
    • Targeted molecular dynamics: A new approach for searching pathways of conformational transitions
    • DOI 10.1016/0263-7855(94)80072-3
    • Schlitter, J., Engels, M., and Krüger, P. (1994) Targeted molecular dynamics: A new approach for searching pathways of conformational transitions J. Mol. Graphics 12, 84-89 (Pubitemid 24219247)
    • (1994) Journal of Molecular Graphics , vol.12 , Issue.2 , pp. 84-89
    • Schlitter, J.1    Engels, M.2    Kruger, P.3
  • 32
  • 33
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • DOI 10.1002/prot.340230412
    • Frishman, D. and Argos, P. (1995) Knowledge-based protein secondary structure assignment Proteins 23, 566-579 (Pubitemid 26009520)
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22, 4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell, R. B. and Barton, G. J. (1992) Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels Proteins 14, 309-323
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 38
    • 13844266306 scopus 로고    scopus 로고
    • Evolutionary profiles derived from the QR factorization of multiple structural alignments gives an economy of information
    • DOI 10.1016/j.jmb.2004.11.053
    • O'Donoghue, P. and Luthey-Schulten, Z. (2005) Evolutionary profiles derived from the qr factorization of multiple structural alignments gives an economy of information J. Mol. Biol. 346, 875-894 (Pubitemid 40247724)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.3 , pp. 875-894
    • O'Donoghue, P.1    Luthey-Schulten, Z.2
  • 39
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: Applications of AutoDock
    • Goodsell, D. S., Morris, G. M., and Olson, A. J. (1996) Automated docking of flexible ligands: Applications of Autodock J. Mol. Recognit. 9, 1-5 (Pubitemid 126565462)
    • (1996) Journal of Molecular Recognition , vol.9 , Issue.1 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 40
    • 33947716119 scopus 로고    scopus 로고
    • Software news and update a semiempirical free energy force field with charge-based desolvation
    • DOI 10.1002/jcc.20634
    • Huey, R., Morris, G. M., Olson, A. J., and Goodsell, D. S. (2007) A semiempirical free energy force field with charge-based desolvation J. Comput. Chem. 28, 1145-1152 (Pubitemid 46506716)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 41
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris, G. M., Goodsell, D. S., Huey, R., and Olson, A. J. (1996) Distributed automated docking of flexible ligands to proteins: Parallel applications of Autodock 2.4 J. Comput.-Aided Mol. Des. 10, 293-304 (Pubitemid 126712824)
    • (1996) Journal of Computer-Aided Molecular Design , vol.10 , Issue.4 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 42
    • 0036137713 scopus 로고    scopus 로고
    • Automated docking to multiple target structures: Incorporation of protein mobility and structural water heterogeneity in autodock
    • DOI 10.1002/prot.10028
    • Osterberg, F., Morris, G. M., Sanner, M. F., Olson, A. J., and Goodsell, D. S. (2002) Automated docking to multiple target structures: Incorporation of protein mobility and structural water heterogeneity in Autodock Proteins 46, 34-40 (Pubitemid 34033574)
    • (2002) Proteins: Structure, Function and Genetics , vol.46 , Issue.1 , pp. 34-40
    • Osterberg, F.1    Morris, G.M.2    Sanner, M.F.3    Olson, A.J.4    Goodsell, D.S.5
  • 43
    • 0346264740 scopus 로고    scopus 로고
    • Automated docking of ligands to an artificial active site: Augmenting crystallographic analysis with computer modeling
    • DOI 10.1023/B:JCAM.0000004604.87558.02
    • Rosenfeld, R. J., Goodsell, D. S., Musah, R. A., Morris, G. M., and Goodin, D. B. 2003, Automated docking of ligands to an artificial active site: Augmenting crystallographic analysis with computer modeling J. Comput.-Aided Mol. Des. 17, 525-536 (Pubitemid 38008964)
    • (2003) Journal of Computer-Aided Molecular Design , vol.17 , Issue.8 , pp. 525-536
    • Rosenfeld, R.J.1    Goodsell, D.S.2    Musah, R.A.3    Morris, G.M.4    Goodin, D.B.5    Olson, A.J.6
  • 44
    • 23044503311 scopus 로고    scopus 로고
    • ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein
    • DOI 10.1021/bi050705j
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2005) ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein Biochemistry 44, 10250-10258 (Pubitemid 41076820)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10250-10258
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 45
    • 0030779102 scopus 로고    scopus 로고
    • Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12
    • DOI 10.1074/jbc.272.34.20986
    • Loo, T. W. and Clarke, D. M. (1997) Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12 J. Biol. Chem. 272, 20986-20989 (Pubitemid 27373952)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.34 , pp. 20986-20989
    • Loo, T.W.1    Clarke, D.M.2
  • 46
    • 0035943691 scopus 로고    scopus 로고
    • Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris(2-maleimidoethyl)amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix
    • Loo, T. W. and Clarke, D. M. (2001) Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris(2-maleimidoethyl)amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix J. Biol. Chem. 276, 31800-31805
    • (2001) J. Biol. Chem. , vol.276 , pp. 31800-31805
    • Loo, T.W.1    Clarke, D.M.2
  • 47
    • 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., and Clarke, D. M. (2008) 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) J. Biol. Chem. , vol.283 , pp. 28190-28197
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 48
    • 80053091327 scopus 로고    scopus 로고
    • Snapshots of the maltose transporter during ATP hydrolysis
    • Oldham, M. L. and Chen, J. (2011) Snapshots of the maltose transporter during ATP hydrolysis Proc. Natl. Acad. Sci. U.S.A. 108, 15152-15156
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15152-15156
    • Oldham, M.L.1    Chen, J.2
  • 49
    • 7244240754 scopus 로고    scopus 로고
    • 12 ATP-binding cassette (ABC) transporter BtuCD
    • DOI 10.1074/jbc.M405084200
    • Oloo, E. O. and Tieleman, D. P. (2004) Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD J. Biol. Chem. 279, 45013-45019 (Pubitemid 39430915)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 45013-45019
    • Oloo, E.O.1    Tieleman, D.P.2
  • 50
    • 41549102797 scopus 로고    scopus 로고
    • Computational models for prediction of interactions with ABC-transporters
    • Ecker, G. F., Stockner, T., and Chiba, P. (2008) Computational models for prediction of interactions with ABC-transporters Drug Discovery Today 13, 311-317
    • (2008) Drug Discovery Today , vol.13 , pp. 311-317
    • Ecker, G.F.1    Stockner, T.2    Chiba, P.3
  • 51
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA
    • DOI 10.1021/bi027337t
    • Campbell, J. D., Biggin, P. C., Baaden, M., and Sansom, M. S. P. (2003) Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA Biochemistry 42, 3666-3673 (Pubitemid 36406372)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.P.4
  • 53
    • 47049126229 scopus 로고    scopus 로고
    • Identification of putative binding sites of P-glycoprotein based on its homology model
    • Globisch, C., Pajeva, I. K., and Wiese, M. (2008) Identification of putative binding sites of P-glycoprotein based on its homology model ChemMedChem 3, 280-295
    • (2008) ChemMedChem , vol.3 , pp. 280-295
    • Globisch, C.1    Pajeva, I.K.2    Wiese, M.3
  • 54
    • 48749107151 scopus 로고    scopus 로고
    • Structural insights into P-glycoprotein (ABCB1) by small angle X-ray scattering and electron crystallography
    • McDevitt, C. A., Shintre, C. A., Günter Grossmann, J., Pollock, N. L., and Prince, S. M. 2008, Structural insights into P-glycoprotein (ABCB1) by small angle X-ray scattering and electron crystallography FEBS Lett. 582, 2950-2956
    • (2008) FEBS Lett. , vol.582 , pp. 2950-2956
    • McDevitt, C.A.1    Shintre, C.A.2    Günter Grossmann, J.3    Pollock, N.L.4    Prince, S.M.5
  • 55
    • 34548133239 scopus 로고    scopus 로고
    • P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK
    • DOI 10.1016/j.febslet.2007.07.069, PII S0014579307008393
    • O'Mara, M. L. and Tieleman, D. P. (2007) P-Glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK FEBS Lett. 581, 4217-4222 (Pubitemid 47301854)
    • (2007) FEBS Letters , vol.581 , Issue.22 , pp. 4217-4222
    • O'Mara, M.L.1    Tieleman, D.P.2
  • 56
    • 33744902318 scopus 로고    scopus 로고
    • Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism
    • DOI 10.1529/biophysj.105.077743
    • Omote, H. and Al-Shawi, M. K. (2006) Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism Biophys. J. 90, 4046-4059 (Pubitemid 43846120)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 4046-4059
    • Omote, H.1    Al-Shawi, M.K.2
  • 57
    • 2342533129 scopus 로고    scopus 로고
    • Structure-Function Relationships of Multidrug Resistance P-Glycoprotein
    • DOI 10.1021/jm031009p
    • Pajeva, I. K., Globisch, C., and Wiese, M. (2004) Structure-function relationships of multidrug resistance P-glycoprotein J. Med. Chem. 47, 2523-2533 (Pubitemid 38580090)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.10 , pp. 2523-2533
    • Pajeva, I.K.1    Globisch, C.2    Wiese, M.3
  • 58
    • 70449713662 scopus 로고    scopus 로고
    • Comparison of the inward- and outward-open homology models and ligand binding of human P-glycoprotein
    • Pajeva, I. K., Globisch, C., and Wiese, M. (2009) Comparison of the inward- and outward-open homology models and ligand binding of human P-glycoprotein FEBS J. 276, 7016-7026
    • (2009) FEBS J. , vol.276 , pp. 7016-7026
    • Pajeva, I.K.1    Globisch, C.2    Wiese, M.3
  • 59
    • 70349512492 scopus 로고    scopus 로고
    • Binding site of ABC transporter homology models confirmed by ABCB1 crystal structure
    • Ravna, A. W., Sylte, I., and Sager, G. (2009) Binding site of ABC transporter homology models confirmed by ABCB1 crystal structure Theor. Biol. Med. Modell. 6, 20
    • (2009) Theor. Biol. Med. Modell. , vol.6 , pp. 20
    • Ravna, A.W.1    Sylte, I.2    Sager, G.3
  • 60
    • 79953236980 scopus 로고    scopus 로고
    • Homology modeling and binding site assessment of the human P-glycoprotein
    • Tarcsay, A. and Keseru, G. M. (2011) Homology modeling and binding site assessment of the human P-glycoprotein Future Med. Chem. 3, 297-307
    • (2011) Future Med. Chem. , vol.3 , pp. 297-307
    • Tarcsay, A.1    Keseru, G.M.2
  • 61
    • 31844443618 scopus 로고    scopus 로고
    • The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding
    • DOI 10.1016/j.febslet.2005.12.051, PII S0014579305015346, ABC Transporters
    • Ambudkar, S. V., Kim, I., Xia, D., and Sauna, Z. E. (2006) The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding FEBS Lett. 580, 1049-1055 (Pubitemid 43185285)
    • (2006) FEBS Letters , vol.580 , Issue.4 , pp. 1049-1055
    • Ambudkar, S.V.1    Kim, I.-W.2    Xia, D.3    Sauna, Z.E.4
  • 62
    • 79952272763 scopus 로고    scopus 로고
    • Probing the stereoselectivity of P-glycoprotein-synthesis, biological activity and ligand docking studies of a set of enantiopure benzopyrano[3,4-b] [1,4]oxazines
    • Jabeen, I., Wetwitayaklung, P., Klepsch, F., Parveen, Z., and Chiba, P. 2011, Probing the stereoselectivity of P-glycoprotein-synthesis, biological activity and ligand docking studies of a set of enantiopure benzopyrano[3,4-b] [1,4]oxazines Chem. Commun. 47, 2586-2588
    • (2011) Chem. Commun. , vol.47 , pp. 2586-2588
    • Jabeen, I.1    Wetwitayaklung, P.2    Klepsch, F.3    Parveen, Z.4    Chiba, P.5
  • 63
    • 80053552409 scopus 로고    scopus 로고
    • Predicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoprotein
    • Bikadi, Z., Hazai, I., Malik, D., Jemnitz, K., and Veres, Z. 2011, Predicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoprotein PLoS One 6, e25815
    • (2011) PLoS One , vol.6 , pp. 25815
    • Bikadi, Z.1    Hazai, I.2    Malik, D.3    Jemnitz, K.4    Veres, Z.5
  • 64
    • 33646541093 scopus 로고    scopus 로고
    • The occluded nucleotide conformation of P-glycoprotein
    • DOI 10.1007/s10863-005-9498-4
    • Tombline, G. and Senior, A. E. (2005) The occluded nucleotide conformation of P-glycoprotein J. Bioenerg. Biomembr. 37, 497-500 (Pubitemid 43725182)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.6 , pp. 497-500
    • Tombline, G.1    Senior, A.E.2
  • 65
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • DOI 10.1111/j.1365-2958.2007.05792.x
    • Dawson, R. J. P., Hollenstein, K., and Locher, K. P. (2007) Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism Mol. Microbiol. 65, 250-257 (Pubitemid 47052721)
    • (2007) Molecular Microbiology , vol.65 , Issue.2 , pp. 250-257
    • Dawson, R.J.P.1    Hollenstein, K.2    Locher, K.P.3
  • 66
    • 4644265234 scopus 로고    scopus 로고
    • The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium
    • DOI 10.1021/bi049045t
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2004) The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium Biochemistry 43, 12081-12089 (Pubitemid 39280552)
    • (2004) Biochemistry , vol.43 , Issue.38 , pp. 12081-12089
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 68
    • 0037131184 scopus 로고    scopus 로고
    • Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains
    • DOI 10.1074/jbc.M206871200
    • Lee, J., Urbatsch, I. L., Senior, A. E., and Wilkens, S. (2002) Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains J. Biol. Chem. 277, 40125-40131 (Pubitemid 35191004)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 40125-40131
    • Lee, J.-Y.1    Urbatsch, I.L.2    Senior, A.E.3    Wilkens, S.4
  • 69
    • 41949129746 scopus 로고    scopus 로고
    • Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy
    • Lee, J., Urbatsch, I. L., Senior, A. E., and Wilkens, S. (2008) Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy J. Biol. Chem. 283, 5769-5779
    • (2008) J. Biol. Chem. , vol.283 , pp. 5769-5779
    • Lee, J.1    Urbatsch, I.L.2    Senior, A.E.3    Wilkens, S.4
  • 70
    • 77951877993 scopus 로고    scopus 로고
    • Human P-glycoprotein is active when the two halves are clamped together in the closed conformation
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2010) Human P-glycoprotein is active when the two halves are clamped together in the closed conformation Biochem. Biophys. Res. Commun. 395, 436-440
    • (2010) Biochem. Biophys. Res. Commun. , vol.395 , pp. 436-440
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 71
    • 79953173207 scopus 로고    scopus 로고
    • P-Glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends
    • Verhalen, B. and Wilkens, S. (2011) P-Glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends J. Biol. Chem. 286, 10476-10482
    • (2011) J. Biol. Chem. , vol.286 , pp. 10476-10482
    • Verhalen, B.1    Wilkens, S.2
  • 72
    • 77649160276 scopus 로고    scopus 로고
    • The gates of ion channels and enzymes
    • Zhou, H. and McCammon, J. A. (2010) The gates of ion channels and enzymes Trends Biochem. Sci. 35, 179-185
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 179-185
    • Zhou, H.1    McCammon, J.A.2
  • 74
    • 0032788590 scopus 로고    scopus 로고
    • Amino acid neighbours and detailed conformational analysis of cysteines in proteins
    • Petersen, M. T., Jonson, P. H., and Petersen, S. B. (1999) Amino acid neighbours and detailed conformational analysis of cysteines in proteins Protein Eng. 12, 535-548 (Pubitemid 29368960)
    • (1999) Protein Engineering , vol.12 , Issue.7 , pp. 535-548
    • Petersen, M.T.N.1    Jonson, P.H.2    Petersen, S.B.3
  • 75
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil
    • Loo, T. W. and Clarke, D. M. (2001) Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil J. Biol. Chem. 276, 14972-14979
    • (2001) J. Biol. Chem. , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 76
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P- glycoprotein using a thiol-reactive substrate
    • DOI 10.1074/jbc.272.51.31945
    • Loo, T. W. and Clarke, D. M. (1997) Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate J. Biol. Chem. 272, 31945-31948 (Pubitemid 28011858)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 77
    • 0033544851 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding domain of human P-glycoprotein: Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane
    • Loo, T. W. and Clarke, D. M. (1999) Identification of residues in the drug-binding domain of human P-glycoprotein. Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane J. Biol. Chem. 274, 35388-35392 (Pubitemid 129512828)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35388-35392
    • Loo, T.W.1    Clarke, D.M.2
  • 78
    • 0034671916 scopus 로고    scopus 로고
    • Identification of residues within the drug-binding domain of the human multidrug resistance P-glycoprotein by cysteine-scanning mutagenesis and reaction with dibromobimane
    • DOI 10.1074/jbc.M007741200
    • Loo, T. W. and Clarke, D. M. (2000) Identification of residues within the drug-binding domain of the human multidrug resistance P-glycoprotein by cysteine-scanning mutagenesis and reaction with dibromobimane J. Biol. Chem. 275, 39272-39278 (Pubitemid 32058947)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39272-39278
    • Loo, T.W.1    Clarke, D.M.2
  • 79
    • 0347379911 scopus 로고    scopus 로고
    • Methanethiosulfonate Derivatives of Rhodamine and Verapamil Activate Human P-glycoprotein at Different Sites
    • DOI 10.1074/jbc.M310448200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites J. Biol. Chem. 278, 50136-50141 (Pubitemid 37548851)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50136-50141
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 80
    • 0038419822 scopus 로고    scopus 로고
    • Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site
    • DOI 10.1074/jbc.C300154200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site J. Biol. Chem. 278, 20449-20452 (Pubitemid 36806339)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20449-20452
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 81
    • 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., and Clarke, D. M. (2009) 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) J. Biol. Chem. , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 82
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: Direct evidence for the substrate-induced fit mechanism for drug binding
    • DOI 10.1074/jbc.C300073200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding J. Biol. Chem. 278, 13603-13606 (Pubitemid 36799891)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 84
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • Loo, T. W. and Clarke, D. M. (2008) Mutational analysis of ABC proteins Arch. Biochem. Biophys. 476, 51-64
    • (2008) Arch. Biochem. Biophys. , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 85
    • 33846419807 scopus 로고    scopus 로고
    • How can we best use structural information on P-glycoprotein to design inhibitors?
    • DOI 10.1016/j.pharmthera.2006.10.003, PII S0163725806001860
    • McDevitt, C. A. and Callaghan, R. (2007) How can we best use structural information on P-glycoprotein to design inhibitors? Pharmacol. Ther. 113, 429-441 (Pubitemid 46149055)
    • (2007) Pharmacology and Therapeutics , vol.113 , Issue.2 , pp. 429-441
    • McDevitt, C.A.1    Callaghan, R.2
  • 86
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • DOI 10.1016/j.sbi.2007.07.003, PII S0959440X07001029
    • Hollenstein, K., Dawson, R. J., and Locher, K. P. (2007) Structure and mechanism of ABC transporter proteins Curr. Opin. Struct. Biol. 17, 412-418 (Pubitemid 47451766)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 412-418
    • Hollenstein, K.1    Dawson, R.J.2    Locher, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.