메뉴 건너뛰기




Volumn 5, Issue 8, 1998, Pages 714-720

Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; MUTANT PROTEIN; PROTEIN TYROSINE KINASE;

EID: 0031853167     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/1412     Document Type: Article
Times cited : (293)

References (39)
  • 2
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C., & Eck, M. J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595–602 (1997).
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 3
    • 0027335694 scopus 로고
    • 1H and 15N assignments and secondary structure of the Src SH3 domain
    • Yu, H., Rosen, M. K., & Schreiber, S. L. 1H and 15N assignments and secondary structure of the Src SH3 domain. FEBS Lett. 324, 87–92 (1993).
    • (1993) FEBS Lett , vol.324 , pp. 87-92
    • Yu, H.1    Rosen, M.K.2    Schreiber, S.L.3
  • 4
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the stability of proteins
    • Pace, N. C., Shirley, B. A., Mcnutt, M. & Gajiwala, K. Forces contributing to the stability of proteins. FASEB 10, 75–83 (1996).
    • (1996) FASEB , vol.10 , pp. 75-83
    • Pace, N.C.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 5
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the src SH3 domain
    • Grantcharova, V. P. & Baker, D. Folding dynamics of the src SH3 domain. Biochemistry 36, 15685–15692 (1998).
    • (1998) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 6
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • Doyle, R., Simons, K., Qian, H. & Baker, D. Local interactions and the optimization of protein folding. Proteins Struct. Func. Gen. 29, 282–291 (1997).
    • (1997) Proteins Struct. Func. Gen. , vol.29 , pp. 282-291
    • Doyle, R.1    Simons, K.2    Qian, H.3    Baker, D.4
  • 7
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N. D., Onuchic, J. N. & Wolynes, P. G. Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104, 5860–5868 (1996).
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 8
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A. R. Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79–84 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 9
    • 0032538302 scopus 로고    scopus 로고
    • Prediction and structure characterization of an independently folding substructure in the src SH3 domain
    • Yi, Q., Bystroff, C. & Baker, D. Prediction and structure characterization of an independently folding substructure in the src SH3 domain. J. Mol. Biol., in the press (1998).
    • (1998) J. Mol. Biol.
    • Yi, Q.1    Bystroff, C.2    Baker, D.3
  • 10
    • 0030900199 scopus 로고    scopus 로고
    • NMR studies of unfolded states of an SH3 domain in acqueos solution and denaturing conditions
    • Zhang, O. & Forman-Kay, J. D. NMR studies of unfolded states of an SH3 domain in acqueos solution and denaturing conditions. Biochemsitry 36, 3959–3970 (1997).
    • (1997) Biochemsitry , vol.36 , pp. 3959-3970
    • Zhang, O.1    Forman-Kay, J.D.2
  • 12
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy
    • Guijarro, J. I., Morton, C., Plaxco, K. W., Campbell, I. D. & Dobson, C. M. Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J. Mol. Biol. 276, 657–667 (1998).
    • (1998) J. Mol. Biol. , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 13
    • 0027361710 scopus 로고
    • Is the slow-exchanging core the protein folding core?
    • Woodward, C. Is the slow-exchanging core the protein folding core? TIBS 18, 359–360 (1993).
    • (1993) TIBS , vol.18 , pp. 359-360
    • Woodward, C.1
  • 14
    • 0031565981 scopus 로고    scopus 로고
    • Contrasting roles for the symmetrically disposed b-turns in the folding of a small protein
    • Gu, H., Kim, D. & Baker, D. Contrasting roles for the symmetrically disposed b-turns in the folding of a small protein. J. Mol. Biol. 274, 588–596 (1997).
    • (1997) J. Mol. Biol. , vol.274 , pp. 588-596
    • Gu, H.1    Kim, D.2    Baker, D.3
  • 15
    • 0031552596 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis
    • Neira, J. L., Itzhaki, L. S., Otzen, D. E., Davis, B. & Fersht, A. R. Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. J. Mol. Biol. 270, 1–12 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 1-12
    • Neira, J.L.1    Itzhaki, L.S.2    Otzen, D.E.3    Davis, B.4    Fersht, A.R.5
  • 16
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., Abkevich, V. & Ptitsyn, O. Conserved residues and the mechanism of protein folding. Nature 379, 96–98 (1996).
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 17
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A.R., Serrano, L. & Wilmanns, M. Different folding transition states may result in the same native structure. Nature Struct. Biol. 3, 874–879 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-879
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 19
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a twostate folding transition
    • Viguera, A. R., Martinez, J. C., Filimonov, V. V., Mateo, P. L., & Serrano, L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a twostate folding transition. Biochemistry 33, 2142–2150 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 20
    • 0031574916 scopus 로고    scopus 로고
    • Non-native interactions in protein folding and stability: Introducing a helical tendency in the all b-sheet a-spectin SH3 domain
    • Prieto, J., Wilmans, M., Jimenez, M. A., Rico, M. & Serrano, L. Non-native interactions in protein folding and stability: introducing a helical tendency in the all b-sheet a-spectin SH3 domain. J. Mol. Biol. 268, 760–778 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 760-778
    • Prieto, J.1    Wilmans, M.2    Jimenez, M.A.3    Rico, M.4    Serrano, L.5
  • 21
    • 0031825181 scopus 로고    scopus 로고
    • Obligatory steps in protein folding and conformational diversity of the transition state
    • Martinez, J. C., Pisabarro, M. T. & Serrano, L. Obligatory steps in protein folding and conformational diversity of the transition state. Nature Struct. Biol. 5, 721–729 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 721-729
    • Martinez, J.C.1    Pisabarro, M.T.2    Serrano, L.3
  • 22
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation condensation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: evidence for a nucleation condensation mechanism for protein folding. J. Mol.Biol. 254, 260–288 (1995).
    • (1995) J. Mol.Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 23
    • 0028882589 scopus 로고
    • P22 Arc Repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M. E., Brown, B. M., Waldburger, C. D. & Sauer, R. T. P22 Arc Repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34, 13914–13919 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 24
    • 0026579572 scopus 로고
    • The folding of an enzyme. 3. Structure of the transition state for unfolding of barnase analyzed by a protein engineering procedure
    • Serrano, L., Matouschek, A. & Fersht, A. The folding of an enzyme. 3. Structure of the transition state for unfolding of barnase analyzed by a protein engineering procedure. J. Mol. Biol. 224, 805–818 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.3
  • 25
    • 0028485627 scopus 로고
    • Protein stability effects of a complete set of alanine substitutions in Arc repressor
    • Milla, M. E., Brown, B. M. & Sauer, R. T. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature Struct. Biol. 1, 518–523 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 518-523
    • Milla, M.E.1    Brown, B.M.2    Sauer, R.T.3
  • 26
    • 0028776642 scopus 로고
    • Matching speed and stability
    • Baldwin, R. L. Matching speed and stability. Nature 369, 183–184 (1994).
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 28
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. & Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10–19 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 31
    • 0030322669 scopus 로고    scopus 로고
    • G. Protein folding funnels: The nature of the transition state ensemble
    • Onuchic, J. N., Socci, N. D., Luthey-Schulten, Z. & Wolynes, P. G. Protein folding funnels: the nature of the transition state ensemble Folding Design 1, 441–450 (1996).
    • (1996) Folding Design , vol.1 , pp. 441-450
    • Onuchic, J.N.1    Socci, N.D.2    Luthey-Schulten, Z.3    Wolynes, P.4
  • 32
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich, V. I., Gutin, A.M. & Shakhnovich, E. I. Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry 33, 10026–10036 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 33
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. & Baker, D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985–994 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.2    Baker, D.3
  • 34
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition state of chymotypsin inhibitor 2 by molecular dynamics simulations
    • Li, A. & Daggett, V. Identification and characterization of the unfolding transition state of chymotypsin inhibitor 2 by molecular dynamics simulations. J. Mol. Biol. 257, 412–429 (1996).
    • (1996) J. Mol. Biol. , vol.257 , pp. 412-429
    • Li, A.1    Daggett, V.2
  • 36
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L
    • Scalley, M. L. et al. Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L. Biochemistry 36, 3373–3382 (1996).
    • (1996) Biochemistry , vol.36 , pp. 3373-3382
    • Scalley, M.L.1
  • 37
    • 0027384577 scopus 로고
    • Effect of cavitycreating mutations in the hdrophobic core of chymotrypsin inhibitor 2
    • Jackson, S. E., Moracci, M., elMarsy, N., Johnson, C. & Fersht, A.R. Effect of cavitycreating mutations in the hdrophobic core of chymotrypsin inhibitor 2. Biochemistry 32, 11259–11269 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    Elmarsy, N.3    Johnson, C.4    Fersht, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.