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Volumn 85, Issue 3, 2014, Pages 420-428

Pore-exposed tyrosine residues of p-glycoprotein are important hydrogen-bonding partners for drugs

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN; MULTIDRUG RESISTANCE PROTEIN; PROPAFENONE; TYROSINE;

EID: 84894024586     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.113.088526     Document Type: Article
Times cited : (32)

References (33)
  • 1
    • 11844297796 scopus 로고    scopus 로고
    • Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas
    • Conseil G, Deeley RG, and Cole SP (2005) Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas. Biochem Pharmacol 69:451-461.
    • (2005) Biochem Pharmacol , vol.69 , pp. 451-461
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.3
  • 2
    • 41549159003 scopus 로고    scopus 로고
    • Multispecificity of drug transporters: Probing inhibitor selectivity for the human drug efflux transporters ABCB1 and ABCG2
    • Cramer J, Kopp S, Bates SE, Chiba P, and Ecker GF (2007) Multispecificity of drug transporters: Probing inhibitor selectivity for the human drug efflux transporters ABCB1 and ABCG2. ChemMedChem 2:1783-1788.
    • (2007) ChemMedChem , vol.2 , pp. 1783-1788
    • Cramer, J.1    Kopp, S.2    Bates, S.E.3    Chiba, P.4    Ecker, G.F.5
  • 3
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJ and Locher KP (2006) Structure of a bacterial multidrug ABC transporter. Nature 443:180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 4
    • 0344761958 scopus 로고    scopus 로고
    • The importance of a nitrogen atom in modulators of multidrug resistance
    • Ecker G, Huber M, Schmid D, and Chiba P (1999) The importance of a nitrogen atom in modulators of multidrug resistance. Mol Pharmacol 56:791-796.
    • (1999) Mol Pharmacol , vol.56 , pp. 791-796
    • Ecker, G.1    Huber, M.2    Schmid, D.3    Chiba, P.4
  • 5
    • 33644672481 scopus 로고    scopus 로고
    • Quantification and characterization of P-glycoprotein-substrate interactions
    • Gatlik-Landwojtowicz E, Aänismaa P, and Seelig A (2006) Quantification and characterization of P-glycoprotein-substrate interactions. Biochemistry 45: 3020-3032.
    • (2006) Biochemistry , vol.45 , pp. 3020-3032
    • Gatlik-Landwojtowicz, E.1    Aänismaa, P.2    Seelig, A.3
  • 7
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: Closing in on the gaps in ABCB1
    • Gutmann DA, Ward A, Urbatsch IL, Chang G, and van Veen HW (2010) Understanding polyspecificity of multidrug ABC transporters: Closing in on the gaps in ABCB1. Trends Biochem Sci 35:36-42.
    • (2010) Trends Biochem Sci , vol.35 , pp. 36-42
    • Gutmann, D.A.1    Ward, A.2    Urbatsch, I.L.3    Chang, G.4    Van Veen, H.W.5
  • 8
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning
    • Hanna M, Brault M, Kwan T, Kast C, and Gros P (1996) Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning. Biochemistry 35: 3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 9
    • 0033676098 scopus 로고    scopus 로고
    • DNA cloning using in vitro sitespecific recombination
    • Hartley JL, Temple GF, and Brasch MA (2000) DNA cloning using in vitro sitespecific recombination. Genome Res 10:1788-1795.
    • (2000) Genome Res , vol.10 , pp. 1788-1795
    • Hartley, J.L.1    Temple, G.F.2    Brasch, M.A.3
  • 10
    • 0035851106 scopus 로고    scopus 로고
    • Mutation of Trp1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2), alters substrate specificity and results in loss of methotrexate transport activity
    • Ito K, Oleschuk CJ, Westlake C, Vasa MZ, Deeley RG, and Cole SP (2001) Mutation of Trp1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2), alters substrate specificity and results in loss of methotrexate transport activity. J Biol Chem 276:38108-38114.
    • (2001) J Biol Chem , vol.276 , pp. 38108-38114
    • Ito, K.1    Oleschuk, C.J.2    Westlake, C.3    Vasa, M.Z.4    Deeley, R.G.5    Cole, S.P.6
  • 11
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • Jin MS, Oldham ML, Zhang Q, and Chen J (2012) Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490:566-569.
    • (2012) Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.3    Chen, J.4
  • 12
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide S and Sidhu SS (2009) The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem Biol 4:325-334.
    • (2009) ACS Chem Biol , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 13
    • 0037147341 scopus 로고    scopus 로고
    • Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1
    • Koike K, Oleschuk CJ, Haimeur A, Olsen SL, Deeley RG, and Cole SP (2002) Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1. J Biol Chem 277:49495-49503.
    • (2002) J Biol Chem , vol.277 , pp. 49495-49503
    • Koike, K.1    Oleschuk, C.J.2    Haimeur, A.3    Olsen, S.L.4    Deeley, R.G.5    Cole, S.P.6
  • 15
    • 84878705648 scopus 로고    scopus 로고
    • The flexibility of P-glycoprotein for its polyspecific drug binding from molecular dynamics simulations
    • Liu M, Hou T, Feng Z, and Li Y (2013) The flexibility of P-glycoprotein for its polyspecific drug binding from molecular dynamics simulations. J Biomol Struct Dyn 31:612-629.
    • (2013) J Biomol Struct Dyn , vol.31 , pp. 612-629
    • Liu, M.1    Hou, T.2    Feng, Z.3    Li, Y.4
  • 16
    • 0034671916 scopus 로고    scopus 로고
    • Identification of residues within the drug-binding domain of the human multidrug resistance P-glycoprotein by cysteinescanning mutagenesis and reaction with dibromobimane
    • Loo TW and Clarke DM (2000) Identification of residues within the drug-binding domain of the human multidrug resistance P-glycoprotein by cysteinescanning mutagenesis and reaction with dibromobimane. J Biol Chem 275: 39272-39278.
    • (2000) J Biol Chem , vol.275 , pp. 39272-39278
    • Loo, T.W.1    Clarke, D.M.2
  • 17
    • 34247626293 scopus 로고    scopus 로고
    • Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment
    • MacCallum JL, Bennett WF, and Tieleman DP (2007) Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment. J Gen Physiol 129:371-377.
    • (2007) J Gen Physiol , vol.129 , pp. 371-377
    • MacCallum, J.L.1    Bennett, W.F.2    Tieleman, D.P.3
  • 19
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • Mian IS, Bradwell AR, and Olson AJ (1991) Structure, function and properties of antibody binding sites. J Mol Biol 217:133-151.
    • (1991) J Mol Biol , vol.217 , pp. 133-151
    • Mian, I.S.1    Bradwell, A.R.2    Olson, A.J.3
  • 23
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labelingprotein homology modeling approach
    • Pleban K, Kopp S, Csaszar E, Peer M, Hrebicek T, Rizzi A, Ecker GF, and Chiba P (2005) P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labelingprotein homology modeling approach. Mol Pharmacol 67:365-374.
    • (2005) Mol Pharmacol , vol.67 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3    Peer, M.4    Hrebicek, T.5    Rizzi, A.6    Ecker, G.F.7    Chiba, P.8
  • 24
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A and Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 25
    • 36849067873 scopus 로고    scopus 로고
    • Catalytic cycle of ATP hydrolysis by P-glycoprotein: Evidence for formation of the E. S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP
    • Sauna ZE, Kim IW, Nandigama K, Kopp S, Chiba P, and Ambudkar SV (2007) Catalytic cycle of ATP hydrolysis by P-glycoprotein: Evidence for formation of the E. S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP. Biochemistry 46:13787-13799.
    • (2007) Biochemistry , vol.46 , pp. 13787-13799
    • Sauna, Z.E.1    Kim, I.W.2    Nandigama, K.3    Kopp, S.4    Chiba, P.5    Ambudkar, S.V.6
  • 26
    • 0032822237 scopus 로고    scopus 로고
    • Structure-activity relationship studies of propafenone analogs based on P-glycoprotein ATPase activity measurements
    • Schmid D, Ecker G, Kopp S, Hitzler M, and Chiba P (1999) Structure-activity relationship studies of propafenone analogs based on P-glycoprotein ATPase activity measurements. Biochem Pharmacol 58:1447-1456.
    • (1999) Biochem Pharmacol , vol.58 , pp. 1447-1456
    • Schmid, D.1    Ecker, G.2    Kopp, S.3    Hitzler, M.4    Chiba, P.5
  • 29
    • 58849086773 scopus 로고    scopus 로고
    • Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains
    • Stockner T, de Vries SJ, Bonvin AM, Ecker GF, and Chiba P (2009) Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains. FEBS J 276:964-972.
    • (2009) FEBS J , vol.276 , pp. 964-972
    • Stockner, T.1    De Vries, S.J.2    Bonvin, A.M.3    Ecker, G.F.4    Chiba, P.5
  • 30
    • 84872144837 scopus 로고    scopus 로고
    • P-glycoprotein is fully active after multiple tryptophan substitutions
    • Swartz DJ, Weber J, and Urbatsch IL (2013) P-glycoprotein is fully active after multiple tryptophan substitutions. Biochim Biophys Acta 1828:1159-1168.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 1159-1168
    • Swartz, D.J.1    Weber, J.2    Urbatsch, I.L.3
  • 31
    • 33745622169 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein ATPase by analogues of tetramethylrosamine: Coupling of drug binding at the "R" site to the ATP hydrolysis transition state
    • Tombline G, Donnelly DJ, Holt JJ, You Y, Ye M, Gannon MK, Nygren CL, and Detty MR (2006) Stimulation of P-glycoprotein ATPase by analogues of tetramethylrosamine: Coupling of drug binding at the "R" site to the ATP hydrolysis transition state. Biochemistry 45:8034-8047.
    • (2006) Biochemistry , vol.45 , pp. 8034-8047
    • Tombline, G.1    Donnelly, D.J.2    Holt, J.J.3    You, Y.4    Ye, M.5    Gannon, M.K.6    Nygren, C.L.7    Detty, M.R.8
  • 32
    • 25444460555 scopus 로고    scopus 로고
    • Involvement of the "occluded nucleotide conformation" of P-glycoprotein in the catalytic pathway
    • Tombline G, Muharemagic A, White LB, and Senior AE (2005) Involvement of the "occluded nucleotide conformation" of P-glycoprotein in the catalytic pathway. Biochemistry 44:12879-12886.
    • (2005) Biochemistry , vol.44 , pp. 12879-12886
    • Tombline, G.1    Muharemagic, A.2    White, L.B.3    Senior, A.E.4
  • 33
    • 53149091283 scopus 로고    scopus 로고
    • Functional analyses reveal an important role for tyrosine residues in the staphylococcal multidrug efflux protein QacA
    • Wu J, Hassan KA, Skurray RA, and Brown MH (2008) Functional analyses reveal an important role for tyrosine residues in the staphylococcal multidrug efflux protein QacA. BMC Microbiol 8:147.
    • (2008) BMC Microbiol , vol.8 , pp. 147
    • Wu, J.1    Hassan, K.A.2    Skurray, R.A.3    Brown, M.H.4


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