메뉴 건너뛰기




Volumn 351, Issue 3, 2005, Pages 672-682

The folding mechanism of a dimeric β-barrel domain

Author keywords

DNA binding; E2; Folding; Papillomavirus; barrel

Indexed keywords

ACID; BINDING PROTEIN; SOLVENT; TRYPTOPHAN; UREA;

EID: 22544472423     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.070     Document Type: Article
Times cited : (17)

References (31)
  • 1
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • R. Jaenicke, and H. Lilie Folding and association of oligomeric and multimeric proteins Advan. Protein Chem. 53 2000 329 401
    • (2000) Advan. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 2
    • 0037058950 scopus 로고    scopus 로고
    • Sequential versus parallel protein-folding mechanisms: Experimental tests for complex folding reactions
    • L.A. Wallace, and C.R. Matthews Sequential versus parallel protein-folding mechanisms: experimental tests for complex folding reactions Biophys. Chem. 101-102 2002 113 131
    • (2002) Biophys. Chem. , vol.101-102 , pp. 113-131
    • Wallace, L.A.1    Matthews, C.R.2
  • 3
    • 0034650515 scopus 로고    scopus 로고
    • The folding pathway of the cell-cycle regulatory protein p13suc1: Clues for the mechanism of domain swapping
    • J.W. Schymkowitz, F. Rousseau, L.R. Irvine, and L.S. Itzhaki The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping Struct. Fold. Des. 8 2000 89 100
    • (2000) Struct. Fold. Des. , vol.8 , pp. 89-100
    • Schymkowitz, J.W.1    Rousseau, F.2    Irvine, L.R.3    Itzhaki, L.S.4
  • 4
    • 0033554860 scopus 로고    scopus 로고
    • Folding and assembly of dimeric human glutathione transferase A1-1
    • L.A. Wallace, and H.W. Dirr Folding and assembly of dimeric human glutathione transferase A1-1 Biochemistry 38 1999 16686 16694
    • (1999) Biochemistry , vol.38 , pp. 16686-16694
    • Wallace, L.A.1    Dirr, H.W.2
  • 5
    • 0035942316 scopus 로고    scopus 로고
    • Folding mechanism of ketosteroid isomerase from Comamonas testosteroni
    • D.H. Kim, D.S. Jang, G.H. Nam, and K.Y. Choi Folding mechanism of ketosteroid isomerase from Comamonas testosteroni Biochemistry 40 2001 5011 5017
    • (2001) Biochemistry , vol.40 , pp. 5011-5017
    • Kim, D.H.1    Jang, D.S.2    Nam, G.H.3    Choi, K.Y.4
  • 6
    • 0025334690 scopus 로고
    • Folding and stability of trp aporepressor from Escherichia coli
    • M.S. Gittelman, and C.R. Matthews Folding and stability of trp aporepressor from Escherichia coli Biochemistry 29 1990 7011 7020
    • (1990) Biochemistry , vol.29 , pp. 7011-7020
    • Gittelman, M.S.1    Matthews, C.R.2
  • 7
    • 0028325298 scopus 로고
    • P22 Arc repressor: Folding kinetics of a single-domain, dimeric protein
    • M.E. Milla, and R.T. Sauer P22 Arc repressor: folding kinetics of a single-domain, dimeric protein Biochemistry 33 1994 1125 1133
    • (1994) Biochemistry , vol.33 , pp. 1125-1133
    • Milla, M.E.1    Sauer, R.T.2
  • 8
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
    • J.A. Zitzewitz, O. Bilsel, J. Luo, B.E. Jones, and C.R. Matthews Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy Biochemistry 34 1995 12812 12819
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5
  • 9
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • R.S. Hegde, S.R. Grossman, L.A. Laimins, and P.B. Sigler Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target Nature 359 1992 505 512
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 10
    • 0036086459 scopus 로고    scopus 로고
    • The papillomavirus E2 proteins: Structure, function, and biology
    • R.S. Hegde The papillomavirus E2 proteins: structure, function, and biology Annu. Rev. Biophys. Biomol. Struct. 31 2002 343 360
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 343-360
    • Hegde, R.S.1
  • 11
    • 0028840956 scopus 로고
    • Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1
    • A. Bochkarev, J.A. Barwell, R.A. Pfuetzner, W. Furey Jr, A.M. Edwards, and L. Frappier Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1 Cell 83 1995 39 46
    • (1995) Cell , vol.83 , pp. 39-46
    • Bochkarev, A.1    Barwell, J.A.2    Pfuetzner, R.A.3    Furey Jr., W.4    Edwards, A.M.5    Frappier, L.6
  • 12
    • 22544471479 scopus 로고    scopus 로고
    • Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric beta-barrel fold
    • A.D. Nadra, T. Eliseo, Y.K. Mok, C.L. Almeida, M. Bycroft, and M. Paci Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric beta-barrel fold J. Biomol. NMR 30 2004 211 214
    • (2004) J. Biomol. NMR , vol.30 , pp. 211-214
    • Nadra, A.D.1    Eliseo, T.2    Mok, Y.K.3    Almeida, C.L.4    Bycroft, M.5    Paci, M.6
  • 13
    • 0030064186 scopus 로고    scopus 로고
    • Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain
    • Y.K. Mok, G. de Prat Gay, P.J. Butler, and M. Bycroft Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain Protein Sci. 5 1996 310 319
    • (1996) Protein Sci. , vol.5 , pp. 310-319
    • Mok, Y.K.1    De Prat Gay, G.2    Butler, P.J.3    Bycroft, M.4
  • 14
    • 0029761636 scopus 로고    scopus 로고
    • The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like
    • Y.K. Mok, M. Bycroft, and G. de Prat-Gay The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like Nature Struct. Biol. 3 1996 711 717
    • (1996) Nature Struct. Biol. , vol.3 , pp. 711-717
    • Mok, Y.K.1    Bycroft, M.2    De Prat-Gay, G.3
  • 15
    • 0034049535 scopus 로고    scopus 로고
    • Folding of a dimeric beta-barrel: Residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain
    • Y.K. Mok, L.G. Alonso, L.M. Lima, M. Bycroft, and G. de Prat-Gay Folding of a dimeric beta-barrel: residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain Protein Sci. 9 2000 799 811
    • (2000) Protein Sci. , vol.9 , pp. 799-811
    • Mok, Y.K.1    Alonso, L.G.2    Lima, L.M.3    Bycroft, M.4    De Prat-Gay, G.5
  • 16
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts
    • M.T. Record Jr, W. Zhang, and C.F. Anderson Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts Advan. Protein Chem. 51 1998 281 353
    • (1998) Advan. Protein Chem. , vol.51 , pp. 281-353
    • Record Jr., M.T.1    Zhang, W.2    Anderson, C.F.3
  • 17
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • B.L. Chen, W.A. Baase, and J.A. Schellman Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations Biochemistry 28 1989 691 699
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 18
    • 0030876594 scopus 로고    scopus 로고
    • Conformational changes and stabilization induced by ligand binding in the DNA-binding domain of the E2 protein from human papillomavirus
    • L.M. Lima, and G. de Prat-Gay Conformational changes and stabilization induced by ligand binding in the DNA-binding domain of the E2 protein from human papillomavirus J. Biol. Chem. 272 1997 19295 19303
    • (1997) J. Biol. Chem. , vol.272 , pp. 19295-19303
    • Lima, L.M.1    De Prat-Gay, G.2
  • 19
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • C.D. Waldburger, T. Jonsson, and R.T. Sauer Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure Proc. Natl Acad. Sci. USA 93 1996 2629 2634
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 20
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • L.S. Itzhaki, P.A. Evans, C.M. Dobson, and S.E. Radford Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes Biochemistry 33 1994 5212 5220
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 21
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 22
    • 0027190920 scopus 로고
    • Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
    • C.J. Mann, and C.R. Matthews Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding Biochemistry 32 1993 5282 5290
    • (1993) Biochemistry , vol.32 , pp. 5282-5290
    • Mann, C.J.1    Matthews, C.R.2
  • 23
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • M.E. Milla, B.M. Brown, C.D. Waldburger, and R.T. Sauer P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding Biochemistry 34 1995 13914 13919
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 25
    • 0032506048 scopus 로고    scopus 로고
    • Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate
    • L.M. Gloss, and C.R. Matthews Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate Biochemistry 37 1998 15990 15999
    • (1998) Biochemistry , vol.37 , pp. 15990-15999
    • Gloss, L.M.1    Matthews, C.R.2
  • 26
    • 0032506169 scopus 로고    scopus 로고
    • The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions
    • L.M. Gloss, and C.R. Matthews The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions Biochemistry 37 1998 16000 16010
    • (1998) Biochemistry , vol.37 , pp. 16000-16010
    • Gloss, L.M.1    Matthews, C.R.2
  • 27
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix↔coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model
    • P.A. Thompson, W.A. Eaton, and J. Hofrichter Laser temperature jump study of the helix↔coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model Biochemistry 36 1997 9200 9210
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 28
    • 0029995708 scopus 로고    scopus 로고
    • Association of complementary fragments and the elucidation of protein folding pathways
    • G. de Prat-Gay Association of complementary fragments and the elucidation of protein folding pathways Protein Eng. 9 1996 843 847
    • (1996) Protein Eng. , vol.9 , pp. 843-847
    • De Prat-Gay, G.1
  • 29
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 30
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 31
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.