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Volumn 5, Issue 1, 1996, Pages 89-97

A recombinant peptide model of the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and ΔF508 mutant forms

Author keywords

autologous folding; cystic fibrosis; mutation; nucleotide binding protein

Indexed keywords

MUTANT PROTEIN; RECOMBINANT PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0030033151     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050111     Document Type: Article
Times cited : (21)

References (54)
  • 1
    • 0026638255 scopus 로고
    • ATP-dependent bacterial transports and cystic fibrosis: Analogy between channels and transporters
    • Ames GFL, Lecar H. 1992. ATP-dependent bacterial transports and cystic fibrosis: Analogy between channels and transporters. FASEB J 6:2660-2666.
    • (1992) FASEB J , vol.6 , pp. 2660-2666
    • Ames, G.F.L.1    Lecar, H.2
  • 2
    • 0026667894 scopus 로고
    • Regulation by ATP and ADP of CFTR chloride channels in the apical membrane of normal and cystic fibrosis airway and intestinal epithelia
    • Anderson MP, Welsh MJ. 1992. Regulation by ATP and ADP of CFTR chloride channels in the apical membrane of normal and cystic fibrosis airway and intestinal epithelia. Science 257:1701-1704.
    • (1992) Science , vol.257 , pp. 1701-1704
    • Anderson, M.P.1    Welsh, M.J.2
  • 3
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator
    • Bear CE, Li C, Kartner N, Bridges RJ, Jensen TJ, Ramjeesingh M, Riordan JR. 1992. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator. Cell 68:809-818.
    • (1992) Cell , vol.68 , pp. 809-818
    • Bear, C.E.1    Li, C.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5    Ramjeesingh, M.6    Riordan, J.R.7
  • 4
    • 0027255319 scopus 로고
    • 5′-Adenylylimidodiphosphate does not activate CFTR chloride channels in cell-free patches of membrane
    • Carson M, Welsh M. 1993. 5′-Adenylylimidodiphosphate does not activate CFTR chloride channels in cell-free patches of membrane. Am J Physiol 265:L27-L32.
    • (1993) Am J Physiol , vol.265
    • Carson, M.1    Welsh, M.2
  • 6
    • 0018110116 scopus 로고
    • Prediction of secondary structure of proteins from their amino acid sequence
    • Chou PY, Fasman GD. 1978. Prediction of secondary structure of proteins from their amino acid sequence. Adv Enzymol 47:45-148.
    • (1978) Adv Enzymol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning G, Anderson M, Amara J, Marshall J, Smith A, Welsh M. 1992. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358:761-764.
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.1    Anderson, M.2    Amara, J.3    Marshall, J.4    Smith, A.5    Welsh, M.6
  • 9
    • 0028328921 scopus 로고
    • A two-domain model for the R domain of the cystic fibrosis transmembrane conductance regulator based on sequence similarities
    • Dulhanty AM, Riordan JR. 1994. A two-domain model for the R domain of the cystic fibrosis transmembrane conductance regulator based on sequence similarities. FEBS Lett 343:109-114.
    • (1994) FEBS Lett , vol.343 , pp. 109-114
    • Dulhanty, A.M.1    Riordan, J.R.2
  • 10
    • 0020975121 scopus 로고
    • Characterization of transducin from bovine rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin
    • Fung BKK, Nash CR. 1983. Characterization of transducin from bovine rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin. Biochemistry 258: 10503-10510.
    • (1983) Biochemistry , vol.258 , pp. 10503-10510
    • Fung, B.K.K.1    Nash, C.R.2
  • 11
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple method for predicting the secondary structure of globular proteins
    • Garnier J, Osguthorpe DJ, Robson B. 1978. Analysis of the accuracy and implications of simple method for predicting the secondary structure of globular proteins. J Mol Biol 120:97-120.
    • (1978) J Mol Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 12
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 14
    • 0028070453 scopus 로고
    • Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator gating
    • Gunderson KL, Kopito RR. 1994. Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator gating. J Biol Chem 269:19349-19353.
    • (1994) J Biol Chem , vol.269 , pp. 19349-19353
    • Gunderson, K.L.1    Kopito, R.R.2
  • 15
    • 0026702994 scopus 로고
    • Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product
    • Hartman J, Huang Z, Rado TA, Peng S, Jilting T, Muccio DD, Sorsher EJ. 1992. Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product. J Biol Chem 267:6455-6458.
    • (1992) J Biol Chem , vol.267 , pp. 6455-6458
    • Hartman, J.1    Huang, Z.2    Rado, T.A.3    Peng, S.4    Jilting, T.5    Muccio, D.D.6    Sorsher, E.J.7
  • 16
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey JP Jr, Johnson WC Jr. 1981. Information content in the circular dichroism of proteins. Biochemistry 20:1085-1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 18
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis
    • Hwang TC, Nagel G, Nairn AC, Gadsby DC. 1994. Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis. Proc Natl Acad Sci USA 91: 4698-4702.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4698-4702
    • Hwang, T.C.1    Nagel, G.2    Nairn, A.C.3    Gadsby, D.C.4
  • 21
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • Sigman, DS. New York: Academic Press
    • Johnson KA. 1992. Transient-state kinetic analysis of enzyme reaction pathways. In: Sigman, DS. The enzymes, 3rd ed, vol XX. New York: Academic Press. pp 2-62.
    • (1992) The Enzymes, 3rd Ed , vol.20 , pp. 2-62
    • Johnson, K.A.1
  • 23
    • 0029113976 scopus 로고
    • The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as a active ATPase
    • Ko Y, Pedersen P. 1995. The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as a active ATPase. J Biol Chem 270:22093-22096.
    • (1995) J Biol Chem , vol.270 , pp. 22093-22096
    • Ko, Y.1    Pedersen, P.2
  • 24
    • 0027524866 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and ΔF508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein
    • Ko Y, Thomas P, Delannoy M, Pedersen P. 1993. The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and ΔF508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein. J Biol Chem 268:24330-24338.
    • (1993) J Biol Chem , vol.268 , pp. 24330-24338
    • Ko, Y.1    Thomas, P.2    Delannoy, M.3    Pedersen, P.4
  • 25
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli IK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, I.K.1
  • 27
    • 0001159016 scopus 로고
    • Imidodiphosphate and pyrophosphate: Possible biological significance of similar structures
    • Larsen M, Willett R, Yount R. 1969. Imidodiphosphate and pyrophosphate: Possible biological significance of similar structures. Science 166:1510.
    • (1969) Science , vol.166 , pp. 1510
    • Larsen, M.1    Willett, R.2    Yount, R.3
  • 28
    • 0027483610 scopus 로고
    • The cystic fibrosis mutation ΔF508 does not influence the chloride channel activity of CFTR
    • Li C, Ramjeesingh M, Reyes E, Jensen T, Chang X, Rommens J, Bear CE. 1993. The cystic fibrosis mutation ΔF508 does not influence the chloride channel activity of CFTR. Nature Genet 3:311-316.
    • (1993) Nature Genet , vol.3 , pp. 311-316
    • Li, C.1    Ramjeesingh, M.2    Reyes, E.3    Jensen, T.4    Chang, X.5    Rommens, J.6    Bear, C.E.7
  • 31
    • 0029058027 scopus 로고
    • Sequence homologies between nucleotide binding regions of CFTR and G-proteins suggest structural and functional similarities
    • Manavalan P, Dearborn DG, McPherson JM, Smith AE. 1995. Sequence homologies between nucleotide binding regions of CFTR and G-proteins suggest structural and functional similarities. FEBS Lett 366:87-91.
    • (1995) FEBS Lett , vol.366 , pp. 87-91
    • Manavalan, P.1    Dearborn, D.G.2    McPherson, J.M.3    Smith, A.E.4
  • 32
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism data
    • Manavalan P, Johnson WC Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism data. Anal Biochem 167:76-85.
    • (1987) Anal Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 33
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn MV, Tong L, DeVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. 1990. Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins. Science 247:939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 34
    • 0026053770 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura CS, Holbrook SR, Ames GFL. 1991. Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc Natl Acad Sci USA 88:84-88.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 84-88
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.L.3
  • 36
    • 0024332065 scopus 로고
    • Substrate and DNA binding to a 50-residue peptide fragment of DNA polymerase I
    • Mullen GP, Shenbagamurthi P, Mildvan AS. 1989. Substrate and DNA binding to a 50-residue peptide fragment of DNA polymerase I. J Biol Chem 264:19637-19647.
    • (1989) J Biol Chem , vol.264 , pp. 19637-19647
    • Mullen, G.P.1    Shenbagamurthi, P.2    Mildvan, A.S.3
  • 37
    • 0026437322 scopus 로고
    • Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding
    • Quinton PM, Reddy MM. 1992. Control of CFTR chloride conductance by ATP levels through non-hydrolytic binding. Nature 360:79-81.
    • (1992) Nature , vol.360 , pp. 79-81
    • Quinton, P.M.1    Reddy, M.M.2
  • 38
    • 0028923471 scopus 로고
    • Expression and functional properties of the second predicted nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator fused to glutathione-S-transferase
    • Randak C, Roscher AA, Hadorn HB, Assfalg-Machleidt I, Auerswald EA, Machleidt W. 1995. Expression and functional properties of the second predicted nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator fused to glutathione-S-transferase. FEBS Lett 363:189-194.
    • (1995) FEBS Lett , vol.363 , pp. 189-194
    • Randak, C.1    Roscher, A.A.2    Hadorn, H.B.3    Assfalg-Machleidt, I.4    Auerswald, E.A.5    Machleidt, W.6
  • 40
    • 0027481813 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • Riordan JR. 1993. The cystic fibrosis transmembrane conductance regulator. Annu Rev Physiol 55:609-630.
    • (1993) Annu Rev Physiol , vol.55 , pp. 609-630
    • Riordan, J.R.1
  • 44
    • 0028223850 scopus 로고
    • The amino-terminal portion of CFTR forms a regulated chloride channel
    • Sheppard DN, Ostedgaard LS, Rich DP, Welsh MJ. 1994. The amino-terminal portion of CFTR forms a regulated chloride channel. Cell 76:1091-1098.
    • (1994) Cell , vol.76 , pp. 1091-1098
    • Sheppard, D.N.1    Ostedgaard, L.S.2    Rich, D.P.3    Welsh, M.J.4
  • 45
    • 0026658476 scopus 로고
    • Altered protein folding may be the molecular basis of most cases of cystic fibrosis
    • Thomas PJ, Ko YH, Pedersen PL. 1992a. Altered protein folding may be the molecular basis of most cases of cystic fibrosis. FEBS Letters 312:7-9.
    • (1992) FEBS Letters , vol.312 , pp. 7-9
    • Thomas, P.J.1    Ko, Y.H.2    Pedersen, P.L.3
  • 46
    • 0027390125 scopus 로고
    • Effects of the ΔF508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR
    • Thomas PJ, Pedersen PL. 1993. Effects of the ΔF508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR. J Bioeng Biomembr 25:11-19.
    • (1993) J Bioeng Biomembr , vol.25 , pp. 11-19
    • Thomas, P.J.1    Pedersen, P.L.2
  • 47
    • 0026649584 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide
    • Thomas PJ, Shenbagamurthi P, Sondek J, Hullihen JM, Pedersen PL. 1992b. The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide. J Biol Chem 267:5727-5730.
    • (1992) J Biol Chem , vol.267 , pp. 5727-5730
    • Thomas, P.J.1    Shenbagamurthi, P.2    Sondek, J.3    Hullihen, J.M.4    Pedersen, P.L.5
  • 48
    • 0027179469 scopus 로고
    • Interactions of nucleotides with membrane-associated cystic fibrosis transmembrane conductance regulator
    • Travis S, Carson M, Ries D, Welsh M. 1993. Interactions of nucleotides with membrane-associated cystic fibrosis transmembrane conductance regulator. J Biol Chem 268:15336-15339.
    • (1993) J Biol Chem , vol.268 , pp. 15336-15339
    • Travis, S.1    Carson, M.2    Ries, D.3    Welsh, M.4
  • 49
    • 0026641782 scopus 로고
    • The spectrum of cystic fibrosis mutations
    • Tsui LC. 1992. The spectrum of cystic fibrosis mutations. Trends Genetics 8:392-398.
    • (1992) Trends Genetics , vol.8 , pp. 392-398
    • Tsui, L.C.1
  • 50
    • 0028276430 scopus 로고
    • ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: Evidence for a three state gating mechanism
    • Venglarik CJ, Schultz BD, Frizzell RA, Bridges RJ. 1994. ATP alters current fluctuations of cystic fibrosis transmembrane conductance regulator: Evidence for a three state gating mechanism. J Gen Physiol 104: 123-146.
    • (1994) J Gen Physiol , vol.104 , pp. 123-146
    • Venglarik, C.J.1    Schultz, B.D.2    Frizzell, R.A.3    Bridges, R.J.4
  • 51
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- And β-subunits of ATP synthetase, myosin, kinases, and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Savaste M, Runswick MJ, Gay NJ. 1982. Distantly related sequences in the α- and β-subunits of ATP synthetase, myosin, kinases, and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1:945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Savaste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 52
    • 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
  • 54
    • 0030087558 scopus 로고    scopus 로고
    • Expression in E. coli of cytoplasmic portions of the cystic fibrosis transmembrane conductance regulator: Apparent bacterial toxicity of peptides containing R domain sequences
    • Forthcoming
    • Yike I, Zhang Y, Ye J, Dearborn DG. 1996. Expression in E. coli of cytoplasmic portions of the cystic fibrosis transmembrane conductance regulator: Apparent bacterial toxicity of peptides containing R domain sequences. Protein Express Purific. Forthcoming.
    • (1996) Protein Express Purific.
    • Yike, I.1    Zhang, Y.2    Ye, J.3    Dearborn, D.G.4


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