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Volumn 332, Issue 3, 2003, Pages 529-536

Allosteric switching by mutually exclusive folding of protein domains

Author keywords

Allostery; Molecular switch; Natively unfolded; Unfolding

Indexed keywords

BARNASE; HYBRID PROTEIN; UBIQUITIN;

EID: 0042736856     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00925-2     Document Type: Article
Times cited : (72)

References (27)
  • 1
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12:2002;54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 2
    • 0036088602 scopus 로고    scopus 로고
    • The linkage between protein folding and functional cooperativity: Two sides of the same coin
    • Luque I., Leavitt S.A., Friere E. The linkage between protein folding and functional cooperativity: two sides of the same coin. Annu. Rev. Biophys. Biomol. Struct. 31:2002;235-256.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 235-256
    • Luque, I.1    Leavitt, S.A.2    Friere, E.3
  • 4
    • 0035823058 scopus 로고    scopus 로고
    • Solution structure and dynamics of yeast elongin C in complex with a von-Hippel-Lindau peptide
    • Botuyan M.V., Mer G., Yi G.-S., Koth C.M., Case D.A., Edwards A.M., et al. Solution structure and dynamics of yeast elongin C in complex with a von-Hippel-Lindau peptide. J. Mol. Biol. 312:2001;177-186.
    • (2001) J. Mol. Biol. , vol.312 , pp. 177-186
    • Botuyan, M.V.1    Mer, G.2    Yi, G.-S.3    Koth, C.M.4    Case, D.A.5    Edwards, A.M.6
  • 5
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature. 404:2000;151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 6
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Binding allosteric switches from simple binding domains
    • Lim W.A. The modular logic of signaling proteins: binding allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12:2002;61-68.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 7
    • 0015868143 scopus 로고
    • On the reaction between the extracelluar ribonuclease of Bacillus amyloliquefaciens (barnase) and its intracellular inhibitor (barstar)
    • Hartley R.W., Smeaton J.R. On the reaction between the extracelluar ribonuclease of Bacillus amyloliquefaciens (barnase) and its intracellular inhibitor (barstar). J. Biol. Chem. 248:1973;5624-5626.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5624-5626
    • Hartley, R.W.1    Smeaton, J.R.2
  • 8
    • 0034032433 scopus 로고    scopus 로고
    • Stability and folding of the protein complexes of barnase
    • Neira J.L., Vázquez E., Fersht A.R. Stability and folding of the protein complexes of barnase. Eur. J. Biochem. 267:2000;2859-2870.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2859-2870
    • Neira, J.L.1    Vázquez, E.2    Fersht, A.R.3
  • 9
    • 0032546542 scopus 로고    scopus 로고
    • A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease
    • Axe D.D., Foster N.W., Fersht A.R. A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease. Biochemistry. 37:1998;7157-7166.
    • (1998) Biochemistry , vol.37 , pp. 7157-7166
    • Axe, D.D.1    Foster, N.W.2    Fersht, A.R.3
  • 10
    • 0026553768 scopus 로고
    • The folding of an enzyme, II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L., Kellis J.T.J., Cann P., Matouschek A., Fersht A.R. The folding of an enzyme, II. Substructure of barnase and the contribution of different interactions to protein stability. J. Mol. Biol. 224:1992;783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.T.J.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 11
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
    • Vuilleumier S., Sancho J., Loewenthal R., Fersht A.R. Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. Biochemistry. 32:1993;10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 12
    • 0035964184 scopus 로고    scopus 로고
    • Insights into the stability of native and partially folded states of ubiquitin: Effects of cosolvents and denaturants on the thermodynamics of protein folding
    • Jourdan M., Searle M.S. Insights into the stability of native and partially folded states of ubiquitin: effects of cosolvents and denaturants on the thermodynamics of protein folding. Biochemistry. 2001;40.
    • (2001) Biochemistry , pp. 40
    • Jourdan, M.1    Searle, M.S.2
  • 13
    • 0033533387 scopus 로고    scopus 로고
    • Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin
    • Finucane M.D., Woolfson D.N. Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin. Biochemistry. 38:1999;11613-11623.
    • (1999) Biochemistry , vol.38 , pp. 11613-11623
    • Finucane, M.D.1    Woolfson, D.N.2
  • 14
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 15
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on a protein surface
    • Loladze V.V., Ibarra-Molero B., Sanchez-Ruiz J.M., Makhatadze G.I. Engineering a thermostable protein via optimization of charge-charge interactions on a protein surface. Biochemistry. 1999;38.
    • (1999) Biochemistry , pp. 38
    • Loladze, V.V.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 16
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero B., Loladze V.V., Makhatadze G.I., Sanchez-Ruiz J.M. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry. 38:1999;8138-8149.
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 17
    • 0026511653 scopus 로고
    • Dissection of an enzyme by protein engineering
    • Sancho J., Fersht A.R. Dissection of an enzyme by protein engineering. J. Mol. Biol. 224:1992;741-747.
    • (1992) J. Mol. Biol. , vol.224 , pp. 741-747
    • Sancho, J.1    Fersht, A.R.2
  • 20
    • 0026751045 scopus 로고
    • Barnase has subsites that give rise to large rate enhancements
    • Day A.G., Parsonage D., Ebel S., Brown T., Fersht A.R. Barnase has subsites that give rise to large rate enhancements. Biochemistry. 31:1992;6390-6395.
    • (1992) Biochemistry , vol.31 , pp. 6390-6395
    • Day, A.G.1    Parsonage, D.2    Ebel, S.3    Brown, T.4    Fersht, A.R.5
  • 21
    • 0024293097 scopus 로고
    • Barnase and barstar: Expression of its cloned inhibitor permits expression of a cloned ribonuclease
    • Hartley R.W. Barnase and barstar: expression of its cloned inhibitor permits expression of a cloned ribonuclease. J. Mol. Biol. 202:1988;913-915.
    • (1988) J. Mol. Biol. , vol.202 , pp. 913-915
    • Hartley, R.W.1
  • 22
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker B.A., Portman J.J., Wolynes P.G. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl Acad. Sci. USA. 97:2000;8868-8873.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 23
    • 0036398105 scopus 로고    scopus 로고
    • Directed evolution of barnase stability using proteolytic selection
    • Pedersen J.S., Otzen D.E., Kristensen P. Directed evolution of barnase stability using proteolytic selection. J. Mol. Biol. 323:2002;115-123.
    • (2002) J. Mol. Biol. , vol.323 , pp. 115-123
    • Pedersen, J.S.1    Otzen, D.E.2    Kristensen, P.3
  • 24
    • 0035018435 scopus 로고    scopus 로고
    • Cancer chemotherapy-ribonucleases to the rescue
    • Leland P.A., Raines R.T. Cancer chemotherapy-ribonucleases to the rescue. Chem. Biol. 8:2001;405-413.
    • (2001) Chem. Biol. , vol.8 , pp. 405-413
    • Leland, P.A.1    Raines, R.T.2
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 27
    • 0003409056 scopus 로고    scopus 로고
    • C.N. Pace, & J.M. Scholtz. New York: Oxford University Press
    • Pace C.N., Scholtz J.M. Protein Structure: A Practical Approach. 1997;Oxford University Press, New York.
    • (1997) Protein Structure: A Practical Approach


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.