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Volumn 7, Issue 6, 2012, Pages

Folding circular permutants of IL-1β: Route selection driven by functional frustration

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 1BETA; POLYPEPTIDE;

EID: 84861856698     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038512     Document Type: Article
Times cited : (22)

References (45)
  • 1
    • 0037453227 scopus 로고    scopus 로고
    • Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli
    • Arai M, Maki K, Takahashi H, Iwakura M, (2003) Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli. J Mol Biol 328: 273-288.
    • (2003) J Mol Biol , vol.328 , pp. 273-288
    • Arai, M.1    Maki, K.2    Takahashi, H.3    Iwakura, M.4
  • 2
    • 1942505822 scopus 로고    scopus 로고
    • Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation
    • Bulaj G, Koehn RE, Goldenberg DP, (2004) Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation. Protein Sci 13: 1182-1196.
    • (2004) Protein Sci , vol.13 , pp. 1182-1196
    • Bulaj, G.1    Koehn, R.E.2    Goldenberg, D.P.3
  • 4
    • 0029422261 scopus 로고
    • Circular permutation of polypeptide chains: implications for protein folding and stability
    • Heinemann U, Hahn M, (1995) Circular permutation of polypeptide chains: implications for protein folding and stability. Prog Biophys Mol Biol 64: 121-143.
    • (1995) Prog Biophys Mol Biol , vol.64 , pp. 121-143
    • Heinemann, U.1    Hahn, M.2
  • 5
    • 27144510594 scopus 로고    scopus 로고
    • Symmetric connectivity of secondary structure elements enhances the diversity of folding pathways
    • Klimov DK, Thirumalai D, (2005) Symmetric connectivity of secondary structure elements enhances the diversity of folding pathways. J Mol Biol 353: 1171-1186.
    • (2005) J Mol Biol , vol.353 , pp. 1171-1186
    • Klimov, D.K.1    Thirumalai, D.2
  • 6
    • 55549098922 scopus 로고    scopus 로고
    • Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity
    • Haglund E, Lindberg MO, Oliveberg M, (2008) Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity. J Biol Chem 283: 27904-27915.
    • (2008) J Biol Chem , vol.283 , pp. 27904-27915
    • Haglund, E.1    Lindberg, M.O.2    Oliveberg, M.3
  • 7
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • Lindberg M, Tangrot J, Oliveberg M, (2002) Complete change of the protein folding transition state upon circular permutation. Nature Structural Biology 9: 818-822.
    • (2002) Nature Structural Biology , vol.9 , pp. 818-822
    • Lindberg, M.1    Tangrot, J.2    Oliveberg, M.3
  • 10
    • 9944262882 scopus 로고    scopus 로고
    • Analysis of fish IL-1beta and derived peptide sequences indicates conserved structures with species-specific IL-1 receptor binding: implications for pharmacological design
    • Koussounadis AI, Ritchie DW, Kemp GJ, Secombes CJ, (2004) Analysis of fish IL-1beta and derived peptide sequences indicates conserved structures with species-specific IL-1 receptor binding: implications for pharmacological design. Curr Pharm Des 10: 3857-3871.
    • (2004) Curr Pharm Des , vol.10 , pp. 3857-3871
    • Koussounadis, A.I.1    Ritchie, D.W.2    Kemp, G.J.3    Secombes, C.J.4
  • 11
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta
    • Vigers GP, Anderson LJ, Caffes P, Brandhuber BJ, (1997) Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature 386: 190-194.
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 12
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta
    • Clementi C, Jennings PA, Onuchic JN, (2000) How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta. Proc Natl Acad Sci U S A 97: 5871-5876.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 13
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1 beta
    • Heidary DK, Gross LA, Roy M, Jennings PA, (1997) Evidence for an obligatory intermediate in the folding of interleukin-1 beta. Nat Struct Biol 4: 725-731.
    • (1997) Nat Struct Biol , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 15
    • 34147140748 scopus 로고    scopus 로고
    • Biophysical characterization of structural properties and folding of interleukin-1 receptor antagonist
    • Latypov RF, Harvey TS, Liu D, Bondarenko PV, Kohno T, et al. (2007) Biophysical characterization of structural properties and folding of interleukin-1 receptor antagonist. J Mol Biol 368: 1187-1201.
    • (2007) J Mol Biol , vol.368 , pp. 1187-1201
    • Latypov, R.F.1    Harvey, T.S.2    Liu, D.3    Bondarenko, P.V.4    Kohno, T.5
  • 18
    • 54449086396 scopus 로고    scopus 로고
    • Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?
    • Capraro DT, Roy M, Onuchic JN, Jennings PA, (2008) Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta? Proc Natl Acad Sci U S A 105: 14844-14848.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14844-14848
    • Capraro, D.T.1    Roy, M.2    Onuchic, J.N.3    Jennings, P.A.4
  • 20
    • 84861875452 scopus 로고    scopus 로고
    • The beta-Bulge Triggers Route-Switching on the Functional Landscape of IL-1 beta
    • in press
    • Capraro DT, (2011) The beta-Bulge Triggers Route-Switching on the Functional Landscape of IL-1 beta. Proc Natl Acad Sci U S A in press.
    • (2011) Proc Natl Acad Sci U S A
    • Capraro, D.T.1
  • 21
    • 0026684334 scopus 로고
    • Permuteins of Interleukin-1-Beta - a Simplified Approach for the Construction of Permutated Proteins Having New Termini
    • Horlick RA, George HJ, Cooke GM, Tritch RJ, Newton RC, et al. (1992) Permuteins of Interleukin-1-Beta- a Simplified Approach for the Construction of Permutated Proteins Having New Termini. Protein Engineering 5: 427-431.
    • (1992) Protein Engineering , vol.5 , pp. 427-431
    • Horlick, R.A.1    George, H.J.2    Cooke, G.M.3    Tritch, R.J.4    Newton, R.C.5
  • 22
    • 84863115565 scopus 로고    scopus 로고
    • Deciphering the preference and predicting the viability of circular permutations in proteins
    • Lo WC, Dai T, Liu YY, Wang LF, Hwang JK, et al. (2012) Deciphering the preference and predicting the viability of circular permutations in proteins. PLoS One 7: e31791.
    • (2012) PLoS One , vol.7
    • Lo, W.C.1    Dai, T.2    Liu, Y.Y.3    Wang, L.F.4    Hwang, J.K.5
  • 23
    • 16244417212 scopus 로고    scopus 로고
    • The native energy landscape for interleukin-1 beta. Modulation of the population ensemble through native-state topology
    • Roy M, Chavez LL, Finke JM, Heidary DK, Onuchic JN, et al. (2005) The native energy landscape for interleukin-1 beta. Modulation of the population ensemble through native-state topology. Journal of Molecular Biology 348: 335-347.
    • (2005) Journal of Molecular Biology , vol.348 , pp. 335-347
    • Roy, M.1    Chavez, L.L.2    Finke, J.M.3    Heidary, D.K.4    Onuchic, J.N.5
  • 24
    • 0037414459 scopus 로고    scopus 로고
    • Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1 beta
    • Roy M, Jennings PA, (2003) Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1 beta. Journal of Molecular Biology 328: 693-703.
    • (2003) Journal of Molecular Biology , vol.328 , pp. 693-703
    • Roy, M.1    Jennings, P.A.2
  • 25
    • 0036304410 scopus 로고    scopus 로고
    • Three topologically equivalent core residues affect the transition state ensemble in a protein folding reaction
    • Heidary DK, Jennings PA, (2002) Three topologically equivalent core residues affect the transition state ensemble in a protein folding reaction. Journal of Molecular Biology 316: 789-798.
    • (2002) Journal of Molecular Biology , vol.316 , pp. 789-798
    • Heidary, D.K.1    Jennings, P.A.2
  • 26
    • 0035688271 scopus 로고    scopus 로고
    • Early aggregated states in the folding of interleukin-1 beta
    • Finke JM, Jennings PA, (2001) Early aggregated states in the folding of interleukin-1 beta. Journal of Biological Physics 27: 119-131.
    • (2001) Journal of Biological Physics , vol.27 , pp. 119-131
    • Finke, J.M.1    Jennings, P.A.2
  • 28
    • 0028561835 scopus 로고
    • Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
    • Jones BE, Jennings PA, Pierre RA, Matthews CR, (1994) Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry (Mosc) 33: 15250-15258.
    • (1994) Biochemistry (Mosc) , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre, R.A.3    Matthews, C.R.4
  • 29
    • 0026096545 scopus 로고
    • Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
    • Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, et al. (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31: 119-128.
    • (1991) Biopolymers , vol.31 , pp. 119-128
    • Semisotnov, G.V.1    Rodionova, N.A.2    Razgulyaev, O.I.3    Uversky, V.N.4    Gripas, A.F.5
  • 32
    • 0031204549 scopus 로고    scopus 로고
    • Interleukin-1 beta-induced expression of protein kinase C (PKC)-delta and epsilon in NIH 3T3 cells
    • Varley CL, Brown BL, Groome N, Dobson PRM, (1997) Interleukin-1 beta-induced expression of protein kinase C (PKC)-delta and epsilon in NIH 3T3 cells. Cytokine 9: 577-581.
    • (1997) Cytokine , vol.9 , pp. 577-581
    • Varley, C.L.1    Brown, B.L.2    Groome, N.3    Dobson, P.R.M.4
  • 33
    • 0035830487 scopus 로고    scopus 로고
    • Different circular permutations produced different folding nuclei in proteins: A computational study
    • Li L, Shakhnovich EI, (2001) Different circular permutations produced different folding nuclei in proteins: A computational study. Journal of Molecular Biology 306: 121-132.
    • (2001) Journal of Molecular Biology , vol.306 , pp. 121-132
    • Li, L.1    Shakhnovich, E.I.2
  • 34
    • 0035824886 scopus 로고    scopus 로고
    • Folding of circular permutants with decreased contact order: General trend balanced by protein stability
    • Lindberg MO, Tangrot J, Otzen DE, Dolgikh DA, Finkelstein AV, et al. (2001) Folding of circular permutants with decreased contact order: General trend balanced by protein stability. J Mol Biol 314: 891-900.
    • (2001) J Mol Biol , vol.314 , pp. 891-900
    • Lindberg, M.O.1    Tangrot, J.2    Otzen, D.E.3    Dolgikh, D.A.4    Finkelstein, A.V.5
  • 35
    • 0000195671 scopus 로고
    • Natural Abundance N-15 Nmr by Enhanced Heteronuclear Spectroscopy
    • Bodenhausen G, Ruben DJ, (1980) Natural Abundance N-15 Nmr by Enhanced Heteronuclear Spectroscopy. Chemical Physics Letters 69: 185-189.
    • (1980) Chemical Physics Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 36
    • 0029338320 scopus 로고
    • Improved Sensitivity of Hsqc Spectra of Exchanging Protons at Short Interscan Delays Using a New Fast Hsqc (Fhsqc) Detection Scheme That Avoids Water Saturation
    • Mori S, Abeygunawardana C, Johnson MO, Vanzijl PCM, (1995) Improved Sensitivity of Hsqc Spectra of Exchanging Protons at Short Interscan Delays Using a New Fast Hsqc (Fhsqc) Detection Scheme That Avoids Water Saturation. Journal of Magnetic Resonance Series B 108: 94-98.
    • (1995) Journal of Magnetic Resonance Series B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Vanzijl, P.C.M.4
  • 37
    • 0027569483 scopus 로고
    • Amino-Acid Type Determination in the Sequential Assignment Procedure of Uniformly C-13/N-15-Enriched Proteins
    • Grzesiek S, Bax A, (1993) Amino-Acid Type Determination in the Sequential Assignment Procedure of Uniformly C-13/N-15-Enriched Proteins. Journal of Biomolecular Nmr 3: 185-204.
    • (1993) Journal of Biomolecular Nmr , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 38
    • 0001689741 scopus 로고
    • Gradient-Enhanced Triple-Resonance 3-Dimensional Nmr Experiments with Improved Sensitivity
    • Muhandiram DR, Kay LE, (1994) Gradient-Enhanced Triple-Resonance 3-Dimensional Nmr Experiments with Improved Sensitivity. Journal of Magnetic Resonance Series B 103: 203-216.
    • (1994) Journal of Magnetic Resonance Series B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 39
    • 0001682998 scopus 로고
    • A 3d Triple-Resonance Nmr Technique for Qualitative Measurement of Carbonyl-H-Beta J Couplings in Isotopically Enriched Proteins
    • Grzesiek S, Ikura M, Clore GM, Gronenborn AM, Bax A, (1992) A 3d Triple-Resonance Nmr Technique for Qualitative Measurement of Carbonyl-H-Beta J Couplings in Isotopically Enriched Proteins. Journal of Magnetic Resonance 96: 215-221.
    • (1992) Journal of Magnetic Resonance , vol.96 , pp. 215-221
    • Grzesiek, S.1    Ikura, M.2    Clore, G.M.3    Gronenborn, A.M.4    Bax, A.5
  • 40
    • 0024448151 scopus 로고
    • Calculation of Protein Extinction Coefficients from Amino-Acid Sequence Data
    • Gill SC, Vonhippel PH, (1989) Calculation of Protein Extinction Coefficients from Amino-Acid Sequence Data. Analytical Biochemistry 182: 319-326.
    • (1989) Analytical Biochemistry , vol.182 , pp. 319-326
    • Gill, S.C.1    Vonhippel, P.H.2
  • 41
    • 84861875456 scopus 로고
    • Protein engineering: a practical approach. Oxford; New York: IRL Press at Oxford University Press
    • Rees AR, Sternberg MJE, Wetzel R, (1992) Protein engineering: a practical approach. Oxford; New York: IRL Press at Oxford University Press. xxv: 397.
    • (1992) , vol.xxv , pp. 397
    • Rees, A.R.1    Sternberg, M.J.E.2    Wetzel, R.3
  • 42
  • 43
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 44
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard TD, Kneller DG, (2008) SPARKY 3, University of California, San Francisco.
    • (2008) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.