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Volumn 1768, Issue 2, 2007, Pages 324-335

Hydrogen-bond formation of the residue in H-loop of the nucleotide binding domain 2 with the ATP in this site and/or other residues of multidrug resistance protein MRP1 plays a crucial role during ATP-dependent solute transport

Author keywords

ATP binding hydrolysis; ATP dependent solute transport; Hydrogen bond; MRP1; Nucleotide binding domain (NBD)

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUTAMIC ACID; GLYCINE; HISTIDINE; LYSINE; MULTIDRUG RESISTANCE PROTEIN 1; NUCLEOTIDE BINDING PROTEIN; PHOSPHATE; SERINE; THREONINE; WATER;

EID: 33846367006     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.11.009     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano R.L., and Ling V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta 455 (1976) 152-162
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 2
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen C.J., Chin J.E., Ueda K., Clark D.P., Pastan I., Gottesman M.M., and Roninson I.B. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47 (1986) 381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 3
    • 0032404092 scopus 로고    scopus 로고
    • A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance
    • Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., and Dean M. A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance. Cancer Res. 58 (1998) 5337-5339
    • (1998) Cancer Res. , vol.58 , pp. 5337-5339
    • Allikmets, R.1    Schriml, L.M.2    Hutchinson, A.3    Romano-Spica, V.4    Dean, M.5
  • 5
    • 0023278796 scopus 로고
    • Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin
    • Mirski S.E., Gerlach J.H., and Cole S.P. Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin. Cancer Res. 47 (1987) 2594-2598
    • (1987) Cancer Res. , vol.47 , pp. 2594-2598
    • Mirski, S.E.1    Gerlach, J.H.2    Cole, S.P.3
  • 7
    • 0023019651 scopus 로고
    • Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance
    • Gerlach J.H., Endicott J.A., Juranka P.F., Henderson G., Sarangi F., Deuchars K.L., and Ling V. Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance. Nature 324 (1986) 485-489
    • (1986) Nature , vol.324 , pp. 485-489
    • Gerlach, J.H.1    Endicott, J.A.2    Juranka, P.F.3    Henderson, G.4    Sarangi, F.5    Deuchars, K.L.6    Ling, V.7
  • 8
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros P., Croop J., and Housman D. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47 (1986) 371-380
    • (1986) Cell , vol.47 , pp. 371-380
    • Gros, P.1    Croop, J.2    Housman, D.3
  • 10
    • 0030863293 scopus 로고    scopus 로고
    • Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus
    • Hipfner D.R., Almquist K.C., Leslie E.M., Gerlach J.H., Grant C.E., Deeley R.G., and Cole S.P. Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J. Biol. Chem. 272 (1997) 23623-23630
    • (1997) J. Biol. Chem. , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3    Gerlach, J.H.4    Grant, C.E.5    Deeley, R.G.6    Cole, S.P.7
  • 12
    • 0034081847 scopus 로고    scopus 로고
    • The multidrug-resistant phenotype associated with overexpression of the new ABC half-transporter, MXR (ABCG2)
    • Litman T., Brangi M., Hudson E., Fetsch P., Abati A., Ross D.D., Miyake K., Resau J.H., and Bates S.E. The multidrug-resistant phenotype associated with overexpression of the new ABC half-transporter, MXR (ABCG2). J. Cell Sci. 113 Pt. 11 (2000) 2011-2021
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 11 , pp. 2011-2021
    • Litman, T.1    Brangi, M.2    Hudson, E.3    Fetsch, P.4    Abati, A.5    Ross, D.D.6    Miyake, K.7    Resau, J.H.8    Bates, S.E.9
  • 13
    • 0037050736 scopus 로고    scopus 로고
    • Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization
    • Kage K., Tsukahara S., Sugiyama T., Asada S., Ishikawa E., Tsuruo T., and Sugimoto Y. Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization. Int. J. Cancer 97 (2002) 626-630
    • (2002) Int. J. Cancer , vol.97 , pp. 626-630
    • Kage, K.1    Tsukahara, S.2    Sugiyama, T.3    Asada, S.4    Ishikawa, E.5    Tsuruo, T.6    Sugimoto, Y.7
  • 14
    • 0345688604 scopus 로고    scopus 로고
    • Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2)
    • Doyle L.A., and Ross D.D. Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2). Oncogene 22 (2003) 7340-7358
    • (2003) Oncogene , vol.22 , pp. 7340-7358
    • Doyle, L.A.1    Ross, D.D.2
  • 15
    • 0345735768 scopus 로고    scopus 로고
    • Functional characterization of human breast cancer resistance protein (BCRP, ABCG2) expressed in the oocytes of Xenopus laevis
    • Nakanishi T., Doyle L.A., Hassel B., Wei Y., Bauer K.S., Wu S., Pumplin D.W., Fang H.B., and Ross D.D. Functional characterization of human breast cancer resistance protein (BCRP, ABCG2) expressed in the oocytes of Xenopus laevis. Mol. Pharmacol. 64 (2003) 1452-1462
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1452-1462
    • Nakanishi, T.1    Doyle, L.A.2    Hassel, B.3    Wei, Y.4    Bauer, K.S.5    Wu, S.6    Pumplin, D.W.7    Fang, H.B.8    Ross, D.D.9
  • 16
    • 0347755373 scopus 로고    scopus 로고
    • Multidrug resistance in cancer chemotherapy and xenobiotic protection mediated by the half ATP-binding cassette transporter ABCG2
    • Han B., and Zhang J.T. Multidrug resistance in cancer chemotherapy and xenobiotic protection mediated by the half ATP-binding cassette transporter ABCG2. Curr. Med. Chem. Anti-Cancer Agents 4 (2004) 31-42
    • (2004) Curr. Med. Chem. Anti-Cancer Agents , vol.4 , pp. 31-42
    • Han, B.1    Zhang, J.T.2
  • 18
    • 27644480743 scopus 로고    scopus 로고
    • Role of the breast cancer resistance protein (ABCG2) in drug transport
    • Mao Q., and Unadkat J.D. Role of the breast cancer resistance protein (ABCG2) in drug transport. AAPS J. 7 (2005) E118-E133
    • (2005) AAPS J. , vol.7
    • Mao, Q.1    Unadkat, J.D.2
  • 19
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1
    • Gao M., Cui H.R., Loe D.W., Grant C.E., Almquist K.C., Cole S.P., and Deeley R.G. Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 275 (2000) 13098-13108
    • (2000) J. Biol. Chem. , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.R.2    Loe, D.W.3    Grant, C.E.4    Almquist, K.C.5    Cole, S.P.6    Deeley, R.G.7
  • 20
    • 0034617097 scopus 로고    scopus 로고
    • Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1
    • Hou Y., Cui L., Riordan J.R., and Chang X.B. Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J. Biol. Chem. 275 (2000) 20280-20287
    • (2000) J. Biol. Chem. , vol.275 , pp. 20280-20287
    • Hou, Y.1    Cui, L.2    Riordan, J.R.3    Chang, X.B.4
  • 21
    • 0042733322 scopus 로고    scopus 로고
    • ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport
    • Yang R., Cui L., Hou Y.-X., Riordan J.R., and Chang X.B. ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport. J. Biol. Chem. 278 (2003) 30764-30771
    • (2003) J. Biol. Chem. , vol.278 , pp. 30764-30771
    • Yang, R.1    Cui, L.2    Hou, Y.-X.3    Riordan, J.R.4    Chang, X.B.5
  • 22
    • 0037085302 scopus 로고    scopus 로고
    • ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain
    • Hou Y.X., Cui L., Riordan J.R., and Chang X.B. ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain. J. Biol. Chem. 277 (2002) 5110-5119
    • (2002) J. Biol. Chem. , vol.277 , pp. 5110-5119
    • Hou, Y.X.1    Cui, L.2    Riordan, J.R.3    Chang, X.B.4
  • 23
    • 33745573710 scopus 로고    scopus 로고
    • Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysis
    • Buyse F., Hou Y.X., Vigano C., Zhao Q., Ruysschaert J.M., and Chang X.B. Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysis. Biochem. J. 397 (2006) 121-130
    • (2006) Biochem. J. , vol.397 , pp. 121-130
    • Buyse, F.1    Hou, Y.X.2    Vigano, C.3    Zhao, Q.4    Ruysschaert, J.M.5    Chang, X.B.6
  • 24
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody J.E., Millen L., Binns D., Hunt J.F., and Thomas P.J. Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277 (2002) 21111-21114
    • (2002) J. Biol. Chem. , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 25
    • 0141755312 scopus 로고    scopus 로고
    • Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)
    • Payen L.F., Gao M., Westlake C.J., Cole S.P., and Deeley R.G. Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1). J. Biol. Chem. 278 (2003) 38537-38547
    • (2003) J. Biol. Chem. , vol.278 , pp. 38537-38547
    • Payen, L.F.1    Gao, M.2    Westlake, C.J.3    Cole, S.P.4    Deeley, R.G.5
  • 27
    • 10344236531 scopus 로고    scopus 로고
    • Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1
    • Zhao Q., and Chang X.B. Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1. J. Biol. Chem. 279 (2004) 48505-48512
    • (2004) J. Biol. Chem. , vol.279 , pp. 48505-48512
    • Zhao, Q.1    Chang, X.B.2
  • 28
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., and Hunt J.F. ATP binding to the motor domain from an ABC transporter drives 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    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 29
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewein S., Jumpertz T., Holland I.B., and Schmitt L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24 (2005) 1901-1910
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 30
    • 21744431708 scopus 로고    scopus 로고
    • Functional interactions between nucleotide binding domains and leukotriene c4 binding sites of multidrug resistance protein 1 (ABCC1)
    • Payen L., Gao M., Westlake C., Theis A., Cole S.P., and Deeley R.G. Functional interactions between nucleotide binding domains and leukotriene c4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 67 (2005) 1944-1953
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1944-1953
    • Payen, L.1    Gao, M.2    Westlake, C.3    Theis, A.4    Cole, S.P.5    Deeley, R.G.6
  • 31
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein [published erratum appears in J Biol Chem 1998 Mar 27;273(13):7782]
    • Chang X.B., Hou Y.X., and Riordan J.R. ATPase activity of purified multidrug resistance-associated protein [published erratum appears in J Biol Chem 1998 Mar 27;273(13):7782]. J. Biol. Chem. 272 (1997) 30962-30968
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 32
    • 0028347079 scopus 로고
    • Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells
    • Leier I., Jedlitschky G., Buchholz U., and Keppler D. Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells. Eur. J. Biochem. 220 (1994) 599-606
    • (1994) Eur. J. Biochem. , vol.220 , pp. 599-606
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Keppler, D.4
  • 33
    • 0030009305 scopus 로고    scopus 로고
    • Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport
    • Loe D.W., Almquist K.C., Deeley R.G., and Cole S.P. Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport. J. Biol. Chem. 271 (1996) 9675-9682
    • (1996) J. Biol. Chem. , vol.271 , pp. 9675-9682
    • Loe, D.W.1    Almquist, K.C.2    Deeley, R.G.3    Cole, S.P.4
  • 34
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung L.W., Wang I.X., Nikaido K., Liu P.Q., Ames G.F., and Kim S.H. 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    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 35
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J., Lu G., Lin J., Davidson A.L., and Quiocho F.A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12 (2003) 651-661
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 36
    • 0028082188 scopus 로고
    • PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1
    • Balzi E., Wang M., Leterme S., Van Dyck L., and Goffeau A. PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1. J. Biol. Chem. 269 (1994) 2206-2214
    • (1994) J. Biol. Chem. , vol.269 , pp. 2206-2214
    • Balzi, E.1    Wang, M.2    Leterme, S.3    Van Dyck, L.4    Goffeau, A.5
  • 37
    • 0025688348 scopus 로고
    • Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters
    • Trowsdale J., Hanson I., Mockridge I., Beck S., Townsend A., and Kelly A. Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters. Nature 348 (1990) 741-744
    • (1990) Nature , vol.348 , pp. 741-744
    • Trowsdale, J.1    Hanson, I.2    Mockridge, I.3    Beck, S.4    Townsend, A.5    Kelly, A.6
  • 38
    • 0028064872 scopus 로고
    • A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein
    • Szczypka M.S., Wemmie J.A., Moye-Rowley W.S., and Thiele D.J. A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein. J. Biol. Chem. 269 (1994) 22853-22857
    • (1994) J. Biol. Chem. , vol.269 , pp. 22853-22857
    • Szczypka, M.S.1    Wemmie, J.A.2    Moye-Rowley, W.S.3    Thiele, D.J.4
  • 40
    • 0037423359 scopus 로고    scopus 로고
    • ATP binding, not hydrolysis, at the first nucleotide-binding domain of multidrug resistance-associated protein MRP1 enhances ADP.Vi trapping at the second domain
    • Hou Y.X., Riordan J.R., and Chang X.B. ATP binding, not hydrolysis, at the first nucleotide-binding domain of multidrug resistance-associated protein MRP1 enhances ADP.Vi trapping at the second domain. J. Biol. Chem. 278 (2003) 3599-3605
    • (2003) J. Biol. Chem. , vol.278 , pp. 3599-3605
    • Hou, Y.X.1    Riordan, J.R.2    Chang, X.B.3
  • 41
    • 29144502288 scopus 로고    scopus 로고
    • ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation
    • Lu G., Westbrooks J.M., Davidson A.L., and Chen J. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17969-17974
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17969-17974
    • Lu, G.1    Westbrooks, J.M.2    Davidson, A.L.3    Chen, J.4
  • 42
    • 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., Craig L., Arthur L.M., Carney J.P., and Tainer J.A. 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    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 43
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs K., Diez J., Greller G., Muller C., Breed J., Schnell C., Vonrhein C., Boos W., and Welte W. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19 (2000) 5951-5961
    • (2000) EMBO J. , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Muller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 44
    • 22244452024 scopus 로고    scopus 로고
    • Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter
    • Zaitseva J., Jenewein S., Wiedenmann A., Benabdelhak H., Holland I.B., and Schmitt L. Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter. Biochemistry 44 (2005) 9680-9690
    • (2005) Biochemistry , vol.44 , pp. 9680-9690
    • Zaitseva, J.1    Jenewein, S.2    Wiedenmann, A.3    Benabdelhak, H.4    Holland, I.B.5    Schmitt, L.6
  • 45
    • 33744791529 scopus 로고    scopus 로고
    • Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site
    • Ramaen O., Leulliot N., Sizun C., Ulryck N., Pamlard O., Lallemand J.Y., Tilbeurgh H., and Jacquet E. Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site. J. Mol. Biol. 359 (2006) 940-949
    • (2006) J. Mol. Biol. , vol.359 , pp. 940-949
    • Ramaen, O.1    Leulliot, N.2    Sizun, C.3    Ulryck, N.4    Pamlard, O.5    Lallemand, J.Y.6    Tilbeurgh, H.7    Jacquet, E.8
  • 46
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • Shyamala V., Baichwal V., Beall E., and Ames G.F. Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations. J. Biol. Chem. 266 (1991) 18714-18719
    • (1991) J. Biol. Chem. , vol.266 , pp. 18714-18719
    • Shyamala, V.1    Baichwal, V.2    Beall, E.3    Ames, G.F.4
  • 47
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido K., and Ames G.F. One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J. Biol. Chem. 274 (1999) 26727-26735
    • (1999) J. Biol. Chem. , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.2
  • 48
    • 0030886132 scopus 로고    scopus 로고
    • Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli
    • Davidson A.L., and Sharma S. Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli. J. Bacteriol. 179 (1997) 5458-5464
    • (1997) J. Bacteriol. , vol.179 , pp. 5458-5464
    • Davidson, A.L.1    Sharma, S.2
  • 49
    • 0027126818 scopus 로고
    • Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family [corrected]
    • Walter C., Wilken S., and Schneider E. Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family [corrected]. FEBS Lett. 303 (1992) 41-44
    • (1992) FEBS Lett. , vol.303 , pp. 41-44
    • Walter, C.1    Wilken, S.2    Schneider, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.