메뉴 건너뛰기




Volumn 69, Issue 21, 2012, Pages 3701-3713

A potentiator induces conformational changes on the recombinant CFTR nucleotide binding domains in solution

Author keywords

ABC transporter; CFTR; Cystic fibrosis; Nucleotide binding domain; Potentiator; Protein stability; Protein structure; X ray scattering

Indexed keywords

2 PYRIMIDIN 7,8 BENZOFLAVONE; ADENOSINE TRIPHOSPHATE; BENZOFLAVONE DERIVATIVE; GUANIDINE; NUCLEOTIDE; RECOMBINANT PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 84867891696     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1049-7     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • Welsh MJ, Smith AE (1993) Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73:1251- 1254
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 2
    • 34347333381 scopus 로고    scopus 로고
    • Molecular targeting of CFTR as a therapeutic approach to cystic fibrosis
    • Amaral MD, Kunzelmann K (2007) Molecular targeting of CFTR as a therapeutic approach to cystic fibrosis. Trends Pharmacol Sci 28:334-341
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 334-341
    • Amaral, M.D.1    Kunzelmann, K.2
  • 3
    • 59349091561 scopus 로고    scopus 로고
    • Chloride channels as drug targets
    • Verkman AS, Galietta LJV (2009) Chloride channels as drug targets. Nat Rev Drug Discov 8:153-171
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 153-171
    • Verkman, A.S.1    Ljv, G.2
  • 7
    • 79960114415 scopus 로고    scopus 로고
    • Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant
    • Yu W, Chiaw PK, Bear CE (2011) Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant. J Biol Chem 286:24714-24725
    • (2011) J Biol Chem , vol.286 , pp. 24714-24725
    • Yu, W.1    Chiaw, P.K.2    Bear, C.E.3
  • 8
    • 79953183131 scopus 로고    scopus 로고
    • Insights into the mechanisms underlying CFTR channel activity, the molecular basis for cystic fibrosis and strategies for therapy
    • Chiaw PK, Eckford PDW, Bear CE (2011) Insights into the mechanisms underlying CFTR channel activity, the molecular basis for cystic fibrosis and strategies for therapy. Essays Biochem 50:233-248
    • (2011) Essays Biochem , vol.50 , pp. 233-248
    • Chiaw, P.K.1    Pdw, E.2    Bear, C.E.3
  • 9
    • 70349847830 scopus 로고    scopus 로고
    • Molecular models of the open and closed states of the whole human CFTR protein
    • Mornon J, Lehn P, Callebaut I (2009) Molecular models of the open and closed states of the whole human CFTR protein. Cell Mol Life Sci 66:3469-3486
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3469-3486
    • Mornon, J.1    Lehn, P.2    Callebaut, I.3
  • 10
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos AW, Hegedus T, Aleksandrov AA, He L, Cui L, Dokholyan NV, Riordan JR (2008) Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc Natl Acad Sci USA 105:3256-3261
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5    Dokholyan, N.V.6    Riordan, J.R.7
  • 13
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by highthroughput screening
    • Pedemonte N, Lukacs GL, Du K, Caci E, Zegarra-Moran O, Galietta LJ, Verkman AS (2005) Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by highthroughput screening. J Clin Invest 115:2564-2571
    • (2005) J Clin Invest , vol.115 , pp. 2564-2571
    • Pedemonte, N.1    Lukacs, G.L.2    Du, K.3    Caci, E.4    Zegarra-Moran, O.5    Galietta, L.J.6    Verkman, A.S.7
  • 17
    • 0035827680 scopus 로고    scopus 로고
    • Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds
    • Galietta LJ, Springsteel MF, Eda M, Niedzinski EJ, By K, Haddadin MJ, Kurth MJ, Nantz MH, Verkman AS (2001) Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds. J Biol Chem 276:19723-19728
    • (2001) J Biol Chem , vol.276 , pp. 19723-19728
    • Galietta, L.J.1    Springsteel, M.F.2    Eda, M.3    Niedzinski, E.J.4    By, K.5    Haddadin, M.J.6    Kurth, M.J.7    Nantz, M.H.8    Verkman, A.S.9
  • 18
    • 10744229649 scopus 로고    scopus 로고
    • Syn thesis, SAR, crystal structure, and biological evaluation of benzoquinoliziniums as activators of wild-type and mutant cystic fibrosis transmembrane conductance regulator channels
    • Marivingt-Mounir C, Norez C, Derand R, Bulteau-Pignoux L, Nguyen-Huy D, Viossat B, Morgant G, Becq F, Vierfond J, Mettey Y (2004) Synthesis, SAR, crystal structure, and biological evaluation of benzoquinoliziniums as activators of wild-type and mutant cystic fibrosis transmembrane conductance regulator channels. J Med Chem 47:962-972
    • (2004) J Med Chem , vol.47 , pp. 962-972
    • Marivingt-Mounir, C.1    Norez, C.2    Derand, R.3    Bulteau-Pignoux, L.4    Nguyen-Huy, D.5    Viossat, B.6    Morgant, G.7    Becq, F.8    Vierfond, J.9    Mettey, Y.10
  • 19
    • 0037205444 scopus 로고    scopus 로고
    • Phloxine B interacts with the cystic fibrosis transmembrane conductance regulator at multiple sites to modulate channel activity
    • Cai Z, Sheppard DN (2002) Phloxine B interacts with the cystic fibrosis transmembrane conductance regulator at multiple sites to modulate channel activity. J Biol Chem 277:19546-19553
    • (2002) J Biol Chem , vol.277 , pp. 19546-19553
    • Cai, Z.1    Sheppard, D.N.2
  • 20
    • 0035141190 scopus 로고    scopus 로고
    • A common mechanism for cystic fibrosis transmembrane conductance regulator protein activation by genistein and benzimidazolone analogs
    • Al-Nakkash L, Hu S, Li M, Hwang TC (2001) A common mechanism for cystic fibrosis transmembrane conductance regulator protein activation by genistein and benzimidazolone analogs. J Pharmacol Exp Ther 296:464-472
    • (2001) J Pharmacol Exp Ther , vol.296 , pp. 464-472
    • Al-Nakkash, L.1    Hu, S.2    Li, M.3    Hwang, T.C.4
  • 22
    • 2442669014 scopus 로고    scopus 로고
    • Capsaicin potentiates wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride-channel currents
    • Ai T, Bompadre SG, Wang X, Hu S, Li M, Hwang T (2004) Capsaicin potentiates wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride-channel currents. Mol Pharmacol 65:1415-1426
    • (2004) Mol Pharmacol , vol.65 , pp. 1415-1426
    • Ai, T.1    Bompadre, S.G.2    Wang, X.3    Hu, S.4    Li, M.5    Hwang, T.6
  • 25
    • 15044353957 scopus 로고    scopus 로고
    • Binding site of activators of the cystic fibrosis transmembrane conductance regulator in the nucleotide binding domains
    • Moran O, Galietta LJV, Zegarra-Moran O (2005) Binding site of activators of the cystic fibrosis transmembrane conductance regulator in the nucleotide binding domains. Cell Mol Life Sci 62:446-460
    • (2005) Cell Mol Life Sci , vol.62 , pp. 446-460
    • Moran, O.1    Ljv, G.2    Zegarra-Moran, O.3
  • 26
    • 34247846123 scopus 로고    scopus 로고
    • Functional analysis of mutations in the putative binding site for cystic fibrosis transmembrane conductance regulator potentiators. Interaction between activation and inhibition
    • Zegarra-Moran O, Monteverde M, Galietta LJV, Moran O (2007) Functional analysis of mutations in the putative binding site for cystic fibrosis transmembrane conductance regulator potentiators. Interaction between activation and inhibition. J Biol Chem 282:9098-9104
    • (2007) J Biol Chem , vol.282 , pp. 9098-9104
    • Zegarra-Moran, O.1    Monteverde, M.2    Ljv, G.3    Moran, O.4
  • 27
    • 78650631518 scopus 로고    scopus 로고
    • Modulation of cystic fibrosis transmembrane conductance regulator (CFTR) activity and genistein binding by cytosolic pH
    • Melani R, Tomatis V, Galietta LJV, Zegarra-Moran O (2010) Modulation of cystic fibrosis transmembrane conductance regulator (CFTR) activity and genistein binding by cytosolic pH. J Biol Chem 285:41591-41596
    • (2010) J Biol Chem , vol.285 , pp. 41591-41596
    • Melani, R.1    Tomatis, V.2    Ljv, G.3    Zegarra-Moran, O.4
  • 28
    • 37249015548 scopus 로고    scopus 로고
    • Characterization of a 7,8- benzoflavone double effect on CFTR Cl(-) channel activity
    • Ferrera L, Pincin C, Moran O (2007) Characterization of a 7,8- benzoflavone double effect on CFTR Cl(-) channel activity. J Membr Biol 220:1-9
    • (2007) J Membr Biol , vol.220 , pp. 1-9
    • Ferrera, L.1    Pincin, C.2    Moran, O.3
  • 29
    • 79959715752 scopus 로고    scopus 로고
    • Small-angle X-ray scattering study of the ATP modulation of the structural features of the nucleotide binding domains of the CFTR in solution
    • Galeno L, Galfre' E, Moran O (2011) Small-angle X-ray scattering study of the ATP modulation of the structural features of the nucleotide binding domains of the CFTR in solution. Eur Biophys J 40:811-824
    • (2011) Eur Biophys J , vol.40 , pp. 811-824
    • Galeno, L.1    Galfre, E.2    Moran, O.3
  • 30
    • 0031426167 scopus 로고    scopus 로고
    • Cystic fibrosis: A disease of altered protein folding
    • Qu BH, Strickland E, Thomas PJ (1997) Cystic fibrosis: a disease of altered protein folding. J Bioenerg Biomembr 29:483-490
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 483-490
    • Qu, B.H.1    Strickland, E.2    Thomas, P.J.3
  • 31
    • 84856733776 scopus 로고    scopus 로고
    • Kinetics of the association/dissociation cycle of an ATP-binding cassette nucleotide-binding domain
    • Zoghbi ME, Fuson KL, Sutton RB, Altenberg GA (2012) Kinetics of the association/dissociation cycle of an ATP-binding cassette nucleotide-binding domain. J Biol Chem 287:4157-4164
    • (2012) J Biol Chem , vol.287 , pp. 4157-4164
    • Zoghbi, M.E.1    Fuson, K.L.2    Sutton, R.B.3    Altenberg, G.A.4
  • 32
    • 0029113976 scopus 로고
    • The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase
    • Ko Y, Pedersen P (1995) The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase. J Biol Chem 270:22093-22096
    • (1995) J Biol Chem , vol.270 , pp. 22093-22096
    • Ko, Y.1    Pedersen, P.2
  • 33
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Pace CN, Shaw KL (2000) Linear extrapolation method of analyzing solvent denaturation curves. Proteins 4:1-7
    • (2000) Proteins , vol.4 , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 34
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 25:495-503
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 35
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas E, Svergun DI (2007) Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J Appl Cryst 40:s245-s249
    • (2007) J Appl Cryst , vol.40
    • Mylonas, E.1    Svergun, D.I.2
  • 36
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: AWindows PC-based system for small-angle scattering data analysis
    • Konarev P, Volkov VV, Sokolova AV, Koch MHJ, Svergun DI (2003) PRIMUS: aWindows PC-based system for small-angle scattering data analysis. J Appl Cryst 36:1277-1282
    • (2003) J Appl Cryst , vol.36 , pp. 1277-1282
    • Konarev, P.1    Volkov, V.V.2    Sokolova, A.V.3    Mhj, K.4    Svergun, D.I.5
  • 37
    • 0035846943 scopus 로고    scopus 로고
    • The overall conformation of conventional kinesins studied by small angle X-ray and neutron scattering
    • Kozielski F, Svergun D, Zaccai G, Wade RH, Koch MH (2001) The overall conformation of conventional kinesins studied by small angle X-ray and neutron scattering. J Biol Chem 276:1267- 1275
    • (2001) J Biol Chem , vol.276 , pp. 1267-1275
    • Kozielski, F.1    Svergun, D.2    Zaccai, G.3    Wade, R.H.4    Koch, M.H.5
  • 38
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab initio shape determination in small-angle scattering
    • Franke D, Svergun DI (2009) DAMMIF, a program for rapid ab initio shape determination in small-angle scattering. J Appl Cryst 42:342-346
    • (2009) J Appl Cryst , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 39
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V, Svergun D (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 36:860-864
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.1    Svergun, D.2
  • 40
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration of multi-resolution structures
    • Wriggers W (2010) Using Situs for the integration of multi-resolution structures. Biophys Rev 2:21-27
    • (2010) Biophys Rev , vol.2 , pp. 21-27
    • Wriggers, W.1
  • 41
    • 4744343547 scopus 로고    scopus 로고
    • A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity
    • Kidd JF, Ramjeesingh M, Stratford F, Huan LJ, Bear CE (2004) A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity. J Biol Chem 279:41664-41669
    • (2004) J Biol Chem , vol.279 , pp. 41664-41669
    • Kidd, J.F.1    Ramjeesingh, M.2    Stratford, F.3    Huan, L.J.4    Bear, C.E.5
  • 45
    • 84857147266 scopus 로고    scopus 로고
    • Transformative mutation specific pharmacotherapy for cystic fibrosis
    • Sanders DB, Farrell PM (2012) Transformative mutation specific pharmacotherapy for cystic fibrosis. BMJ 344:e79
    • (2012) BMJ , vol.344
    • Sanders, D.B.1    Farrell, P.M.2
  • 46
    • 84857021686 scopus 로고    scopus 로고
    • Personalized medicine. New cystic fibrosis drug offers hope, at a price
    • Kaiser J (2012) Personalized medicine. New cystic fibrosis drug offers hope, at a price. Science 335:645
    • (2012) Science , vol.335 , pp. 645
    • Kaiser, J.1
  • 47
    • 84867863472 scopus 로고    scopus 로고
    • Biophysical chemistry
    • Allen J (2008) Biophysical chemistry. Wiley, Oxford
    • (2008) Wiley Oxford
    • Allen, J.1
  • 48
    • 0032954806 scopus 로고    scopus 로고
    • Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme
    • Zeltwanger S, Wang F, Wang GT, Gillis KD, Hwang TC (1999) Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme. J Gen Physiol 113:541-554
    • (1999) J Gen Physiol , vol.113 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.T.3    Gillis, K.D.4    Hwang, T.C.5
  • 49
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide- binding domains
    • Vergani P, Lockless SW, Nairn AC, Gadsby DC (2005) CFTR channel opening by ATP-driven tight dimerization of its nucleotide- binding domains. Nature 433:876-880
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 50
    • 66849129301 scopus 로고    scopus 로고
    • A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability
    • Wellhauser L, Chiaw PK, Pasyk S, Li C, Ramjeesingh M, Bear CE (2009) A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability. Mol Pharmacol 75:1430-1438
    • (2009) Mol Pharmacol , vol.75 , pp. 1430-1438
    • Wellhauser, L.1    Chiaw, P.K.2    Pasyk, S.3    Li, C.4    Ramjeesingh, M.5    Bear, C.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.