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Volumn 47, Issue 32, 2008, Pages 8456-8464

Interaction between the bound Mg·ATP and the Walker a serine residue in NBD2 of multidrug resistance-associated protein MRP1 plays a crucial role for the ATP-dependent leukotriene C4 transport

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HYDROGEN; HYDROGEN BONDS; NONMETALS; STRUCTURAL ANALYSIS;

EID: 49449115300     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8007643     Document Type: Article
Times cited : (8)

References (25)
  • 3
    • 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. (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24 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
  • 4
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • Verdon, G., Albers, S. V., Dijkstra, B. W., Driessen, A. J., and Thunnissen, A. M. (2003) Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J. Mol. Biol. 330, 343-358.
    • (2003) J. Mol. Biol , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 5
    • 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. (2005) ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc. Natl. Acad. Sci. U.S.A. 102, 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
  • 6
    • 33749076230 scopus 로고    scopus 로고
    • Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter
    • Procko, E., Ferrin-O'Connell, I., Ng, S. L., and Gaudet, R. (2006) Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol. Cell 24, 51-62.
    • (2006) Mol. Cell , vol.24 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.L.3    Gaudet, R.4
  • 7
    • 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., Milien, L., Moody, J. E., Rosen, J., Thomas, P. J., and Hunt, J. F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149.
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Milien, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 8
    • 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. (2000) Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J. Biol. Chem. 275, 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
  • 9
    • 0035424958 scopus 로고    scopus 로고
    • Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation
    • Cui, L., Hou, Y. X., Riordan, J. R., and Chang, X. B. (2001) Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation. Arch. Biochem. Biophys. 392, 153-161.
    • (2001) Arch. Biochem. Biophys , vol.392 , pp. 153-161
    • Cui, L.1    Hou, Y.X.2    Riordan, J.R.3    Chang, X.B.4
  • 10
    • 38349065419 scopus 로고    scopus 로고
    • The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function
    • Yang, R., Scavetta, R., and Chang, X. B. (2008) The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function. Biochim. Biophys. Acta 1778, 454-465.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 454-465
    • Yang, R.1    Scavetta, R.2    Chang, X.B.3
  • 11
    • 0030689692 scopus 로고    scopus 로고
    • Chang, X. B., Hou, Y. X., and Riordan, J. R. (1997) ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 272, 30962-30968. [erratum: (1998) J. Biol. Chem. 273, 7782].
    • Chang, X. B., Hou, Y. X., and Riordan, J. R. (1997) ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 272, 30962-30968. [erratum: (1998) J. Biol. Chem. 273, 7782].
  • 12
    • 14544295691 scopus 로고    scopus 로고
    • Nucleotide dissociation from NBD1 promotes solute transport by MRP1
    • Yang, R., McBride, A., Hou, Y. X., Goldberg, A., and Chang, X. B. (2005) Nucleotide dissociation from NBD1 promotes solute transport by MRP1. Biochim. Biophys. Acta 1668, 248-261.
    • (2005) Biochim. Biophys. Acta , vol.1668 , pp. 248-261
    • Yang, R.1    McBride, A.2    Hou, Y.X.3    Goldberg, A.4    Chang, X.B.5
  • 13
    • 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. (2004) 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, 48505-48512.
    • (2004) J. Biol. Chem , vol.279 , pp. 48505-48512
    • Zhao, Q.1    Chang, X.B.2
  • 14
    • 0028347079 scopus 로고
    • Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells
    • Leier, I., Jedlitschky, G., Buchholz, U., and Keppler, D. (1994) Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells. Eur. J. Biochem. 220, 599-606.
    • (1994) Eur. J. Biochem , vol.220 , pp. 599-606
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Keppler, D.4
  • 15
    • 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. 1996a 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, 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
  • 16
    • 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. (2002) 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, 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
  • 17
    • 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. (2003) 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, 3599-3605.
    • (2003) J. Biol. Chem , vol.278 , pp. 3599-3605
    • Hou, Y.X.1    Riordan, J.R.2    Chang, X.B.3
  • 19
    • 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. (2005) Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 67, 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
  • 20
    • 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. (2003) 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, 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
  • 22
    • 0345583699 scopus 로고    scopus 로고
    • Hrycyna, C. A., Ramachandra, M., Germann, U. A., Cheng, P. W., Pastan, 1, and Gottesman, M. M. (1999) Both ATP sites of human P-glycoprotein are essential but not symmetric. Biochemistry 38, 13887-13899.
    • Hrycyna, C. A., Ramachandra, M., Germann, U. A., Cheng, P. W., Pastan, 1, and Gottesman, M. M. (1999) Both ATP sites of human P-glycoprotein are essential but not symmetric. Biochemistry 38, 13887-13899.
  • 23
    • 33847357783 scopus 로고    scopus 로고
    • Misassembled mutant ΔF508 CFTR in the distal secretory pathway alters cellular lipid trafficking
    • Gentzsch, M., Choudhury, A., Chang, X. B., Pagano, R. E., and Riordan, J. R. (2007) Misassembled mutant ΔF508 CFTR in the distal secretory pathway alters cellular lipid trafficking. J. Cell Sci. 120, 447-455.
    • (2007) J. Cell Sci , vol.120 , pp. 447-455
    • Gentzsch, M.1    Choudhury, A.2    Chang, X.B.3    Pagano, R.E.4    Riordan, J.R.5
  • 24
    • 33846367006 scopus 로고    scopus 로고
    • 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
    • Yang, R., and Chang, X. B. (2007) 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. Biochim. Biophys. Acta 1768, 324-335.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 324-335
    • Yang, R.1    Chang, X.B.2
  • 25
    • 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. (2000) Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 275, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.