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Volumn 14, Issue 5, 2005, Pages 1282-1292

Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment

Author keywords

crystallin fold; Age related cataract; Essential dynamics; Principal components analysis; Protein molecular dynamics simulation; Protein stability; Protein unfolding rates

Indexed keywords

BETA B2 CRYSTALLIN; BETA CRYSTALLIN; CRYSTALLIN; CYSTEINE; MUTANT PROTEIN; PHENYLALANINE; UNCLASSIFIED DRUG;

EID: 17744391285     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041227805     Document Type: Article
Times cited : (30)

References (41)
  • 2
    • 0026731884 scopus 로고
    • Structural studies on β H-crystallin from bovine eye lens
    • Bateman, O.A. and Slingsby, C. 1992. Structural studies on β H-crystallin from bovine eye lens. Exp. Eye Res. 55: 127-133.
    • (1992) Exp. Eye Res. , vol.55 , pp. 127-133
    • Bateman, O.A.1    Slingsby, C.2
  • 3
    • 0034771090 scopus 로고    scopus 로고
    • Association behaviour of human βB1-crystallin and its truncated forms
    • Bateman, O.A., Lubsen, N.H., and Slingsby, C. 2001. Association behaviour of human βB1-crystallin and its truncated forms. Exp. Eye Res. 73: 321-331.
    • (2001) Exp. Eye Res. , vol.73 , pp. 321-331
    • Bateman, O.A.1    Lubsen, N.H.2    Slingsby, C.3
  • 7
    • 0019485220 scopus 로고
    • The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II
    • Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, L, Turnell, B., and Wistow, G. 1981. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289: 771-777.
    • (1981) Nature , vol.289 , pp. 771-777
    • Blundell, T.1    Lindley, P.2    Miller, L.3    Moss, D.4    Slingsby, C.5    Tickle, L.6    Turnell, B.7    Wistow, G.8
  • 8
    • 0031472252 scopus 로고    scopus 로고
    • Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway
    • Bond, C.J., Wong, K.B., Clarke, J., Fersht, A.R., and Daggett, V. 1997. Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway. Proc. Natl. Acad. Sci. 94: 13409-13413.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 13409-13413
    • Bond, C.J.1    Wong, K.B.2    Clarke, J.3    Fersht, A.R.4    Daggett, V.5
  • 9
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • Clark, J.I. and Muchowski, P.J. 2000. Small heat-shock proteins and their potential role in human disease. Curr. Opin. Struct. Biol. 10: 52-59.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 10
    • 0034423527 scopus 로고    scopus 로고
    • The N-terminal domain of βB2-crystallin resembles the putative ancestral homodimer
    • Clout, N.J., Basak, A., Wieligmann, K., Bateman, O.A., Jaenicke, R., and Slingsby, C. 2000. The N-terminal domain of βB2-crystallin resembles the putative ancestral homodimer. J. Mol. Biol. 304: 253-257.
    • (2000) J. Mol. Biol. , vol.304 , pp. 253-257
    • Clout, N.J.1    Basak, A.2    Wieligmann, K.3    Bateman, O.A.4    Jaenicke, R.5    Slingsby, C.6
  • 11
    • 0345329408 scopus 로고    scopus 로고
    • Use of essential and molecular dynamics to study γB-crystallin unfolding after non-enzymic post-translational modifications
    • Crabbe, M.J., Cooper, L.R., and Corne, D.W. 2003. Use of essential and molecular dynamics to study γB-crystallin unfolding after non-enzymic post-translational modifications. Comput. Biol. Chem. 27: 507-510.
    • (2003) Comput. Biol. Chem. , vol.27 , pp. 507-510
    • Crabbe, M.J.1    Cooper, L.R.2    Corne, D.W.3
  • 12
    • 0027472047 scopus 로고
    • Evolution of the α-crystallin/small heat-shock protein family
    • de Jong, W.W., Leunissen, J.A., and Voorter, C.E. 1993. Evolution of the α-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10: 103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 13
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye, M. and Tardieu, A. 1983. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302: 415-417.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 14
  • 15
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N. and Peitsch, M.C. 1997. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0000145042 scopus 로고
    • The lens: Development, proteins, metabolism and cataract
    • ed. H. Davson, Academic Press, New York
    • Harding, J.J. and Crabbe, M.J.C. 1984. The lens: Development, proteins, metabolism and cataract. In The eye, 3rd ed. (ed. H. Davson), pp. 207-492. Academic Press, New York.
    • (1984) The Eye, 3rd Ed. , pp. 207-492
    • Harding, J.J.1    Crabbe, M.J.C.2
  • 17
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz, J. 1992. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. 89: 10449-10453.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 19
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: Structure, stability, and function
    • Jaenicke, R. and Slingsby, C. 2001. Lens crystallins and their microbial homologs: Structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36: 435-499.
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 21
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation
    • Kosinski-Collins, M.S. and King, J. 2003. In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation. Protein Sci. 12: 480-490.
    • (2003) Protein Sci. , vol.12 , pp. 480-490
    • Kosinski-Collins, M.S.1    King, J.2
  • 22
    • 3342948291 scopus 로고    scopus 로고
    • Probing folding and fluorescence quenching in human γD crystallin Greek key domains using triple tryptophan mutant proteins
    • Kosinski-Collins, M.S., Flaugh, S.L., and King, J. 2004. Probing folding and fluorescence quenching in human γD crystallin Greek key domains using triple tryptophan mutant proteins. Protein Sci. 13: 2223-2235.
    • (2004) Protein Sci. , vol.13 , pp. 2223-2235
    • Kosinski-Collins, M.S.1    Flaugh, S.L.2    King, J.3
  • 23
    • 0033055093 scopus 로고    scopus 로고
    • Kinetic and thermodynamic stabilization of the βγ-crystallin homolog spherulin 3a from Physarum polycephalum by calcium binding
    • Kretschmar, M., Mayr, E.M., and Jaenicke, R. 1999. Kinetic and thermodynamic stabilization of the βγ-crystallin homolog spherulin 3a from Physarum polycephalum by calcium binding. J. Mol. Biol. 289: 701-705.
    • (1999) J. Mol. Biol. , vol.289 , pp. 701-705
    • Kretschmar, M.1    Mayr, E.M.2    Jaenicke, R.3
  • 25
    • 4644319196 scopus 로고    scopus 로고
    • CDTool - An integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving
    • Lees, J.G., Smith, B.R., Wien, F., Miles, A.J., and Wallace, B.A. 2004. CDTool - An integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving. Anal. Biochem. 332: 285-289.
    • (2004) Anal. Biochem. , vol.332 , pp. 285-289
    • Lees, J.G.1    Smith, B.R.2    Wien, F.3    Miles, A.J.4    Wallace, B.A.5
  • 26
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
    • Makarov, D.E. and Plaxco, K.W. 2003. The topomer search model: A simple, quantitative theory of two-state protein folding kinetics. Protein Sci. 12: 17-26.
    • (2003) Protein Sci. , vol.12 , pp. 17-26
    • Makarov, D.E.1    Plaxco, K.W.2
  • 27
    • 0348147599 scopus 로고    scopus 로고
    • Calibration and standardization of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers
    • Miles, A.J., Wien, F., Lees, J.G., Rodger, A., Janes, R.W., and Wallace, B.A. 2003. Calibration and standardization of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers. Spectroscopy 17: 653-661.
    • (2003) Spectroscopy , vol.17 , pp. 653-661
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Rodger, A.4    Janes, R.W.5    Wallace, B.A.6
  • 28
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D., Welker, C., Schindler, T., Schroder, K., Marahiel, M.A., Jaenicke, R., and Schmid, F.X. 1998. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol. 5: 229-235.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1    Welker, C.2    Schindler, T.3    Schroder, K.4    Marahiel, M.A.5    Jaenicke, R.6    Schmid, F.X.7
  • 29
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 30
    • 0001155770 scopus 로고    scopus 로고
    • Simulation of the highly stable protein: Bovine γB-crystallin at room and high temperature
    • Purkiss, A.G., Slingsby, C., and Goodfellow, J.M. 2000. Simulation of the highly stable protein: Bovine γB-crystallin at room and high temperature. Protein Pept. Lett. 7: 211-217.
    • (2000) Protein Pept. Lett. , vol.7 , pp. 211-217
    • Purkiss, A.G.1    Slingsby, C.2    Goodfellow, J.M.3
  • 31
    • 11144250815 scopus 로고    scopus 로고
    • Comparison of Generalised Born/Surface Area with periodic boundary simulations to study protein unfolding
    • Purkiss, A.G., MacDonald, J.T., Goodfellow, J.M., and Slingsby, C. 2004. Comparison of Generalised Born/Surface Area with periodic boundary simulations to study protein unfolding. Mol. Simul. 30: 335-342.
    • (2004) Mol. Simul. , vol.30 , pp. 335-342
    • Purkiss, A.G.1    MacDonald, J.T.2    Goodfellow, J.M.3    Slingsby, C.4
  • 32
    • 0025339471 scopus 로고
    • Folding of an all-β protein: Independent domain folding in γ II-crystallin from calf eye lens
    • Rudolph, R., Siebendritt, R., Nesslauer, G., Sharma, A.K., and Jaenicke, R. 1990. Folding of an all-β protein: Independent domain folding in γ II-crystallin from calf eye lens. Proc. Natl. Acad. Sci. 87: 4625-4629.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5
  • 33
    • 1942437441 scopus 로고    scopus 로고
    • Binding of destabilized βB2-crystallin mutants to α-crystallin: The role of a folding intermediate
    • Sathish, H.A., Koteiche, H.A., and McHaourab, H.S. 2004. Binding of destabilized βB2-crystallin mutants to α-crystallin: The role of a folding intermediate. J. Biol. Chem. 279: 16425-16432.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16425-16432
    • Sathish, H.A.1    Koteiche, H.A.2    McHaourab, H.S.3
  • 34
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β-crystallins favor heterologous association
    • Slingsby, C. and Bateman, O.A. 1990. Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β-crystallins favor heterologous association. Biochemistry 29: 6592-6599.
    • (1990) Biochemistry , vol.29 , pp. 6592-6599
    • Slingsby, C.1    Bateman, O.A.2
  • 36
    • 0033551420 scopus 로고    scopus 로고
    • Formation of βA3/βB2-crystallin mixed complexes: Involvement of N- and C-terminal extensions
    • Werten, P.J., Lindner, R.A., Carver, J.A., and de Jong, W.W. 1999. Formation of βA3/βB2-crystallin mixed complexes: Involvement of N- and C-terminal extensions. Biochim. Biophys. Acta 1432: 286-292.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 286-292
    • Werten, P.J.1    Lindner, R.A.2    Carver, J.A.3    De Jong, W.W.4
  • 37
    • 0033525632 scopus 로고    scopus 로고
    • Folding and self-assembly of the domains of βB2-crystallin from rat eye lens
    • Wieligmann, K., Mayr, E.M., and Jaenicke, R. 1999. Folding and self-assembly of the domains of βB2-crystallin from rat eye lens. J. Mol. Biol. 286: 989-994.
    • (1999) J. Mol. Biol. , vol.286 , pp. 989-994
    • Wieligmann, K.1    Mayr, E.M.2    Jaenicke, R.3
  • 38
    • 0025117557 scopus 로고
    • Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins
    • Wistow, G. 1990. Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30: 140-145.
    • (1990) J. Mol. Evol. , vol.30 , pp. 140-145
    • Wistow, G.1
  • 40
    • 0021881956 scopus 로고
    • Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens β γ-crystallins
    • Wistow, G., Summers, L., and Blundell, T. 1985. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens β γ-crystallins. Nature 315: 771-773.
    • (1985) Nature , vol.315 , pp. 771-773
    • Wistow, G.1    Summers, L.2    Blundell, T.3
  • 41
    • 0034740569 scopus 로고    scopus 로고
    • Resistance of human βB2-crystallin to in vivo modification
    • Zhang, Z., David, L.L., Smith, D.L., and Smith, J.B. 2001. Resistance of human βB2-crystallin to in vivo modification. Exp. Eye Res. 73: 203-211.
    • (2001) Exp. Eye Res. , vol.73 , pp. 203-211
    • Zhang, Z.1    David, L.L.2    Smith, D.L.3    Smith, J.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.