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Volumn 45, Issue 44, 2006, Pages 13249-13263

Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CRYSTAL STRUCTURE; FLUORESCENCE; HYDROGEN BONDS; MOLECULAR STRUCTURE; X RAY CRYSTALLOGRAPHY;

EID: 33750690511     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0611964     Document Type: Article
Times cited : (55)

References (32)
  • 1
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large (∼700 kDa) caspase-activating complex
    • Cain, K., Brown, D. G., Langlais, C., and Cohen, G. M. (1999) Caspase activation involves the formation of the aposome, a large (∼700 kDa) caspase-activating complex, J. Biol. Chem. 274, 22686-22692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3    Cohen, G.M.4
  • 2
    • 0035960678 scopus 로고    scopus 로고
    • Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer
    • Pop, C., Chen, Y.-R., Smith, B., Bose, K., Bobay, B., Tripathy, A., Franzen, S., and Clark, A. C. (2001) Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer, Biochemistry 40, 14224-14235.
    • (2001) Biochemistry , vol.40 , pp. 14224-14235
    • Pop, C.1    Chen, Y.-R.2    Smith, B.3    Bose, K.4    Bobay, B.5    Tripathy, A.6    Franzen, S.7    Clark, A.C.8
  • 4
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism lor caspase-8 activation
    • Donepudi, M., Sweeney, A. M., Briande, C., and Grutter, M. G. (2003) Insights into the regulatory mechanism lor caspase-8 activation, Mol. Cell 11, 543-549.
    • (2003) Mol. Cell , vol.11 , pp. 543-549
    • Donepudi, M.1    Sweeney, A.M.2    Briande, C.3    Grutter, M.G.4
  • 5
    • 0033596980 scopus 로고    scopus 로고
    • An apaF-1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y., Liu, X., and Wang, X. (1999) An apaF-1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9, J. Biol. Chem. 274, 11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 6
  • 9
    • 0142063422 scopus 로고    scopus 로고
    • An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3
    • Bose, K., Pop, C., Feeney, B., and Clark, A. C. (2003) An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3, Biochemistry 42, 12298-12310.
    • (2003) Biochemistry , vol.42 , pp. 12298-12310
    • Bose, K.1    Pop, C.2    Feeney, B.3    Clark, A.C.4
  • 16
    • 0142242170 scopus 로고    scopus 로고
    • Crystal structure of caspase-2, apical initiator of the intrinsic apopiotic pathway
    • Schweizer, A., Briande, C., and Grutter, M. G. (2003) Crystal structure of caspase-2, apical initiator of the intrinsic apopiotic pathway, J. Biol. Chem. 278, 42441-42447.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42441-42447
    • Schweizer, A.1    Briande, C.2    Grutter, M.G.3
  • 17
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai, J., Wu, Q., Shiozaki, E., Srinivasula, S. M., Alnemri, E. S., und Shi, Y. (2001) Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding, Cell 107, 399-407.
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 19
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity activation and inhibition
    • Fuentes-Prior, P., and Salvesen, G. S. (2004) The protein structures that shape caspase activity, specificity activation and inhibition, Biochem. J. 384, 201-232.
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 20
    • 0142063420 scopus 로고    scopus 로고
    • Mutations in the procaspase-3 dimer interface affect the activity of the zymogen
    • Pop, C., Feeney, B., Tripathy, A., and Clark, A. C. (2003) Mutations in the procaspase-3 dimer interface affect the activity of the zymogen, Biochemistry 42, 12311-12320.
    • (2003) Biochemistry , vol.42 , pp. 12311-12320
    • Pop, C.1    Feeney, B.2    Tripathy, A.3    Clark, A.C.4
  • 21
    • 10944256201 scopus 로고    scopus 로고
    • Ionic interactions near loop L4 are important for maintaining the active site environment and the dimer stability of (pro)caspase-3
    • Feeney, B., Pop, C., Tripathy, A., and Clark, A. C. (2004) Ionic interactions near loop L4 are important for maintaining the active site environment and the dimer stability of (pro)caspase-3, Biochem. J. 384, 515-525.
    • (2004) Biochem. J. , vol.384 , pp. 515-525
    • Feeney, B.1    Pop, C.2    Tripathy, A.3    Clark, A.C.4
  • 22
    • 0032847318 scopus 로고    scopus 로고
    • Caspases: Preparation and characterization
    • Stennicke, H. R., and Salvesen, G. S. (1999) Caspases: Preparation and characterization, Methods 17, 313-319.
    • (1999) Methods , vol.17 , pp. 313-319
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 23
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp apore-pressor using single tryptophan mutants
    • Royer, C. A., Mann, C. J., and Matthews, C. R. (1993) Resolution of the fluorescence equilibrium unfolding profile of trp apore-pressor using single tryptophan mutants, Protein Sci. 2, 1844-1852.
    • (1993) Protein Sci. , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 11144221992 scopus 로고    scopus 로고
    • pH effects on the stability and dimerization of procaspase-3
    • Bose, K., and Clark, A. C. (2005) pH effects on the stability and dimerization of procaspase-3, Protein Sci. 14, 24-36.
    • (2005) Protein Sci. , vol.14 , pp. 24-36
    • Bose, K.1    Clark, A.C.2
  • 27
    • 28844472825 scopus 로고    scopus 로고
    • Reassembly of active caspase-3 is facilitated by the propeptide
    • Feeney, B., and Clark, A. C. (2005) Reassembly of active caspase-3 is facilitated by the propeptide, J. Biol. Chem. 280, 39772-39785.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39772-39785
    • Feeney, B.1    Clark, A.C.2
  • 28
    • 0038306254 scopus 로고    scopus 로고
    • Conformational restrictions in the active site of unliganded human caspase-3
    • Ni, C.-Z., Li, C., Wu, J. C., Spada, A. P., and Ely, K. R. (2003) Conformational restrictions in the active site of unliganded human caspase-3, J. Mol. Recognit. 16, 121-124.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 121-124
    • Ni, C.-Z.1    Li, C.2    Wu, J.C.3    Spada, A.P.4    Ely, K.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.