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Volumn 90, Issue 1, 2016, Pages 35-41

Cryo-EM analysis of the conformational landscape of human P-glycoprotein (ABCB1) during its catalytic cycle

Author keywords

[No Author keywords available]

Indexed keywords

MULTIDRUG RESISTANCE PROTEIN 1; ABCB1 PROTEIN, HUMAN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MULTIDRUG RESISTANCE PROTEIN;

EID: 84976420394     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.116.104190     Document Type: Article
Times cited : (71)

References (37)
  • 2
    • 84856305229 scopus 로고    scopus 로고
    • Catalytic and transport cycles of ABC exporters
    • Al-Shawi MK (2011) Catalytic and transport cycles of ABC exporters. Essays Biochem 50:63-83.
    • (2011) Essays Biochem , vol.50 , pp. 63-83
    • Al-Shawi, M.K.1
  • 3
    • 0032321894 scopus 로고    scopus 로고
    • Drug-stimulatable ATPase activity in crude membranes of human MDR1-transfected mammalian cells
    • Ambudkar SV (1998) Drug-stimulatable ATPase activity in crude membranes of human MDR1-transfected mammalian cells. Methods Enzymol 292:504-514.
    • (1998) Methods Enzymol , vol.292 , pp. 504-514
    • Ambudkar, S.V.1
  • 4
    • 0030868612 scopus 로고    scopus 로고
    • Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein
    • Ambudkar SV, Cardarelli CO, Pashinsky I, and Stein WD (1997) Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein. J Biol Chem 272:21160-21166.
    • (1997) J Biol Chem , vol.272 , pp. 21160-21166
    • Ambudkar, S.V.1    Cardarelli, C.O.2    Pashinsky, I.3    Stein, W.D.4
  • 6
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug-resistance pump: Characterization of the drug-stimulatable ATP hydrolysis
    • Ambudkar SV, Lelong IH, Zhang J, Cardarelli CO, Gottesman MM, and Pastan I (1992) Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci USA 89:8472-8476.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 7
    • 84905974179 scopus 로고    scopus 로고
    • Structure of b-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
    • Bartesaghi A, Matthies D, Banerjee S, Merk A, and Subramaniam S (2014) Structure of b-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy. Proc Natl Acad Sci USA 111:11709-11714.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 11709-11714
    • Bartesaghi, A.1    Matthies, D.2    Banerjee, S.3    Merk, A.4    Subramaniam, S.5
  • 9
    • 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
  • 10
    • 84905040016 scopus 로고    scopus 로고
    • Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
    • Hohl M, Hürlimann LM, Böhm S, Schöppe J, Grütter MG, Bordignon E, and Seeger MA (2014) Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter. Proc Natl Acad Sci USA 111:11025-11030.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 11025-11030
    • Hohl, M.1    Hürlimann, L.M.2    Böhm, S.3    Schöppe, J.4    Grütter, M.G.5    Bordignon, E.6    Seeger, M.A.7
  • 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
    • 0035937707 scopus 로고    scopus 로고
    • Correlation between steady-state ATP hydrolysis and vanadate-induced ADP trapping in Human P-glycoprotein. Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates
    • Kerr KM, Sauna ZE, and Ambudkar SV (2001) Correlation between steady-state ATP hydrolysis and vanadate-induced ADP trapping in Human P-glycoprotein. Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates. J Biol Chem 276:8657-8664.
    • (2001) J Biol Chem , vol.276 , pp. 8657-8664
    • Kerr, K.M.1    Sauna, Z.E.2    Ambudkar, S.V.3
  • 14
    • 84900449189 scopus 로고    scopus 로고
    • Refined structures of mouse P-glycoprotein
    • Li J, Jaimes KF, and Aller SG (2014) Refined structures of mouse P-glycoprotein. Protein Sci 23:34-46.
    • (2014) Protein Sci , vol.23 , pp. 34-46
    • Li, J.1    Jaimes, K.F.2    Aller, S.G.3
  • 15
    • 84864535297 scopus 로고    scopus 로고
    • The ATPase activity of the Pglycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely together
    • Loo TW, Bartlett MC, Detty MR, and Clarke DM (2012) The ATPase activity of the Pglycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely together. J Biol Chem 287:26806-26816.
    • (2012) J Biol Chem , vol.287 , pp. 26806-26816
    • Loo, T.W.1    Bartlett, M.C.2    Detty, M.R.3    Clarke, D.M.4
  • 17
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA and Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 21
    • 0029797074 scopus 로고    scopus 로고
    • Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system
    • Ramachandra M, Ambudkar SV, Gottesman MM, Pastan I, and Hrycyna CA (1996) Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system. Mol Biol Cell 7:1485-1498.
    • (1996) Mol Biol Cell , vol.7 , pp. 1485-1498
    • Ramachandra, M.1    Ambudkar, S.V.2    Gottesman, M.M.3    Pastan, I.4    Hrycyna, C.A.5
  • 22
    • 80655125018 scopus 로고    scopus 로고
    • Conformational analysis of human ATPbinding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2
    • Ritchie TK, Kwon H, and Atkins WM (2011) Conformational analysis of human ATPbinding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2. J Biol Chem 286:39489-39496.
    • (2011) J Biol Chem , vol.286 , pp. 39489-39496
    • Ritchie, T.K.1    Kwon, H.2    Atkins, W.M.3
  • 23
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi B, Price EM, Boucher RC, Germann UA, and Scarborough GA (1992) 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) 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
  • 24
    • 0034646468 scopus 로고    scopus 로고
    • Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
    • Sauna ZE and Ambudkar SV (2000) Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein. Proc Natl Acad Sci USA 97:2515-2520.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2515-2520
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 25
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: How P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • Sauna ZE and Ambudkar SV (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.
    • (2007) Mol Cancer Ther , vol.6 , pp. 13-23
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 26
    • 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
  • 27
    • 33748747880 scopus 로고    scopus 로고
    • Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1)
    • Sauna ZE, Nandigama K, and Ambudkar SV (2006) Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1). J Biol Chem 281:26501-26511.
    • (2006) J Biol Chem , vol.281 , pp. 26501-26511
    • Sauna, Z.E.1    Nandigama, K.2    Ambudkar, S.V.3
  • 28
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH (2012) RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530.
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 29
    • 80053074680 scopus 로고    scopus 로고
    • Reaction chemistry ABC-style
    • Senior AE (2011) Reaction chemistry ABC-style. Proc Natl Acad Sci USA 108: 15015-15016.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15015-15016
    • Senior, A.E.1
  • 30
    • 84901070245 scopus 로고    scopus 로고
    • Complex interplay between the P-Glycoprotein multidrug efflux pump and the membrane: Its role in modulating protein function
    • Sharom FJ (2014) Complex Interplay between the P-Glycoprotein Multidrug Efflux Pump and the Membrane: Its Role in Modulating Protein Function. Front Oncol 4: 41.
    • (2014) Front Oncol , vol.4 , pp. 41
    • Sharom, F.J.1
  • 32
    • 84885991911 scopus 로고    scopus 로고
    • Conserved walker A cysteines 431 and 1074 in human P-glycoprotein are accessible to thiolspecific agents in the apo and ADP-vanadate trapped conformations
    • Sim HM, Bhatnagar J, Chufan EE, Kapoor K, and Ambudkar SV (2013) Conserved Walker A cysteines 431 and 1074 in human P-glycoprotein are accessible to thiolspecific agents in the apo and ADP-vanadate trapped conformations. Biochemistry 52:7327-7338.
    • (2013) Biochemistry , vol.52 , pp. 7327-7338
    • Sim, H.M.1    Bhatnagar, J.2    Chufan, E.E.3    Kapoor, K.4    Ambudkar, S.V.5
  • 35
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch IL, Sankaran B, Weber J, and Senior AE (1995) P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem 270:19383-19390.
    • (1995) J Biol Chem , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 37
    • 84922342044 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Wilkens S (2015) Structure and mechanism of ABC transporters. F1000Prime Rep 7: 14.
    • (2015) F1000Prime Rep , vol.7 , pp. 14
    • Wilkens, S.1


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