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Volumn 22, Issue 3, 2003, Pages 200-204

A new dimer interface for an ABC transporter

Author keywords

ATP binding cassette; LmrA; MsbA; P glycoprotein

Indexed keywords

ABC TRANSPORTER; CARRIER PROTEIN; DIMER; GLYCOPROTEIN P; LIPID A; MONOMER; MSBA PROTEIN; SPIRAL; UNCLASSIFIED DRUG;

EID: 0041833335     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0924-8579(03)00212-7     Document Type: Article
Times cited : (15)

References (16)
  • 1
    • 0032900953 scopus 로고    scopus 로고
    • Biochemical, cellular and pharmacological aspects of the multidrug transporter
    • Ambudkar S.V., Dey S., Hrycyna C.A., et al. Biochemical, cellular and pharmacological aspects of the multidrug transporter. Annu. Rev. Pharmacol. Toxicol. 39:1999;361-398.
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 361-398
    • Ambudkar, S.V.1    Dey, S.2    Hrycyna, C.A.3
  • 2
    • 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., et al. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature. 391:1998;291-295.
    • (1998) Nature , vol.391 , pp. 291-295
    • Van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3
  • 3
    • 85163545088 scopus 로고    scopus 로고
    • I.B. Holland, S.P.C. Cole, K. Kuchler, & C.F. Higgins. London: Academic Press
    • Holland I.B., Cole S.P.C., Kuchler K., Higgins C.F. ABC proteins. From bacteria to man. 2003;Academic Press, London.
    • (2003) ABC proteins. From bacteria to man
  • 4
    • 0035823075 scopus 로고    scopus 로고
    • The structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., Roth C.B. The structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science. 293:2001;1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 5
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • van Veen H.W., Margolles A., Muller M., et al. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J. 19:2000;2503-2514.
    • (2000) EMBO J. , vol.19 , pp. 2503-2514
    • Van Veen, H.W.1    Margolles, A.2    Muller, M.3
  • 6
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis
    • Vigano C., Margolles A., van Veen H.W., et al. Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. J. Biol. Chem. 275:2000;10962-10967.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10962-10967
    • Vigano, C.1    Margolles, A.2    Van Veen, H.W.3
  • 7
    • 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., et al. Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis. J. Biol. Chem. 271:1996;24617-24624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3
  • 8
    • 0027432409 scopus 로고
    • Fluorescent cellular indicators are extruded by the multidrug resistance protein
    • Homolya L., Holl Z., Germann U.A., et al. Fluorescent cellular indicators are extruded by the multidrug resistance protein. J. Biol. Chem. 268:1993;21493-21496.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21493-21496
    • Homolya, L.1    Holl, Z.2    Germann, U.A.3
  • 9
    • 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., et al. Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J. 15:1996;4239-4245.
    • (1996) EMBO J. , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    Van Veen, H.W.2    Molenaar, D.3
  • 10
    • 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. 296:2002;1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 11
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung L.W., Wang I.X., Nikaido K., et al. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 396:1998;703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3
  • 12
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner K.-P., Karcher A., Shin D.S., et al. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell. 101:2000;789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.-P.1    Karcher, A.2    Shin, D.S.3
  • 13
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter druves formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., et al. ATP binding to the motor domain from an ABC transporter druves formation of a nucleotide sandwich dimer. Mol. Cell. 10:2002;139-149.
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3
  • 14
    • 0036829647 scopus 로고    scopus 로고
    • The LSGGQ motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence
    • Loo T.W., Clarke D.M. The LSGGQ motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence. J. Biol. Chem. 277:2002;41303-41306.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Clarke, D.M.2
  • 15
    • 0035813143 scopus 로고    scopus 로고
    • Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers
    • Loo T.W., Clarke D.M. Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers. J. Biol. Chem. 276:2001;36877-36880.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 16
    • 17944370228 scopus 로고    scopus 로고
    • Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle
    • Rosenberg M.F., Velarde G., Ford R.C., et al. Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle. EMBO J. 20:2001;5615-5625.
    • (2001) EMBO J. , vol.20 , pp. 5615-5625
    • Rosenberg, M.F.1    Velarde, G.2    Ford, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.