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Volumn 359, Issue 5, 2006, Pages 1378-1388

Extended Substrate Recognition in Caspase-3 Revealed by High Resolution X-ray Structure Analysis

Author keywords

caspase; low barrier hydrogen bond; radiation damage; safety catch; substrate specificity

Indexed keywords

ASPARTIC ACID; CARBON; CASPASE 3; KETONE; PEPTIDE;

EID: 33745260957     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.04.051     Document Type: Article
Times cited : (51)

References (42)
  • 1
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., and Kaufmann S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Ann. Rev. Biochem. 68 (1999) 383-424
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 2
    • 0034522342 scopus 로고    scopus 로고
    • Caspases: key players in programmed cell death
    • Grutter M.G. Caspases: key players in programmed cell death. Curr. Opin.Struct. Biol. 10 (2000) 649
    • (2000) Curr. Opin.Struct. Biol. , vol.10 , pp. 649
    • Grutter, M.G.1
  • 3
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl S.J., and Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nature Rev. Mol. Cell Biol. 5 (2004) 897-907
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 4
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 Pt 2 (2004) 201-232
    • (2004) Biochem. J. , vol.384 , Issue.PART 2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 5
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6 (1999) 1028-1042
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 6
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T., Garcia-Calvo M., et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272 (1997) 17907-17911
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6
  • 7
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke H.R., Renatus M., Meldal M., and Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350 (2000) 563-568
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 8
    • 0030889913 scopus 로고    scopus 로고
    • Structure of recombinant human CPP32 in complex with the tetrapeptide Acetyl-Asp-Val-Ala-Asp fluoromethyl ketone
    • Mittl P.R.E., Di Marco S., Krebs J.F., Bai X., Karanewsky D.S., Priestle J.P., et al. Structure of recombinant human CPP32 in complex with the tetrapeptide Acetyl-Asp-Val-Ala-Asp fluoromethyl ketone. J. Biol. Chem. 272 (1997) 6539-6547
    • (1997) J. Biol. Chem. , vol.272 , pp. 6539-6547
    • Mittl, P.R.E.1    Di Marco, S.2    Krebs, J.F.3    Bai, X.4    Karanewsky, D.S.5    Priestle, J.P.6
  • 11
    • 3042850072 scopus 로고    scopus 로고
    • Prospects for caspase inhibitors
    • O'Brien T., and Lee D. Prospects for caspase inhibitors. Mini. Rev. Med. Chem. 4 (2004) 153-165
    • (2004) Mini. Rev. Med. Chem. , vol.4 , pp. 153-165
    • O'Brien, T.1    Lee, D.2
  • 13
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter P., and Wells J.A. Dissecting the catalytic triad of a serine protease. Nature 332 (1988) 564
    • (1988) Nature , vol.332 , pp. 564
    • Carter, P.1    Wells, J.A.2
  • 14
    • 0023044226 scopus 로고
    • The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state
    • Polgar L., and Asboth B. The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state. J. Theor. Biol. 121 (1986) 323-326
    • (1986) J. Theor. Biol. , vol.121 , pp. 323-326
    • Polgar, L.1    Asboth, B.2
  • 15
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers J.C., Asgian J.L., Ekici O.D., and James K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102 (2002) 4639-4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 16
    • 0142142211 scopus 로고    scopus 로고
    • Cysteine protease inhibitors containing small rings
    • Schirmeister T., and Klockow A. Cysteine protease inhibitors containing small rings. Mini. Rev. Med. Chem. 3 (2003) 585-596
    • (2003) Mini. Rev. Med. Chem. , vol.3 , pp. 585-596
    • Schirmeister, T.1    Klockow, A.2
  • 17
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer A.C., and Menard R. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244 (1994) 486-500
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 18
    • 0033036804 scopus 로고    scopus 로고
    • A catalytic mechanism for caspase-1 and for bimodal inhibition of caspase-1 by activated aspartic ketones
    • Brady K.D., Giegel D.A., Grinnell C., Lunney E., Talanian R.V., Wong W., and Walker N. A catalytic mechanism for caspase-1 and for bimodal inhibition of caspase-1 by activated aspartic ketones. Bioorg. Med. Chem. 7 (1999) 621-631
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 621-631
    • Brady, K.D.1    Giegel, D.A.2    Grinnell, C.3    Lunney, E.4    Talanian, R.V.5    Wong, W.6    Walker, N.7
  • 20
    • 0036499652 scopus 로고    scopus 로고
    • Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins
    • Aravind L., and Koonin E.V. Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins: Struct. Funct. Genet. 46 (2002) 355-367
    • (2002) Proteins: Struct. Funct. Genet. , vol.46 , pp. 355-367
    • Aravind, L.1    Koonin, E.V.2
  • 21
    • 0034717269 scopus 로고    scopus 로고
    • Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality
    • Lee D., Long S.A., Adams J.L., Chan G., Vaidya K.S., Francis T.A., et al. Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality. J. Biol. Chem. 275 (2000) 16007-16014
    • (2000) J. Biol. Chem. , vol.275 , pp. 16007-16014
    • Lee, D.1    Long, S.A.2    Adams, J.L.3    Chan, G.4    Vaidya, K.S.5    Francis, T.A.6
  • 22
    • 14344272939 scopus 로고    scopus 로고
    • Maintenance of caspase-3 proenzyme dormancy by an intrinsic "safety catch" regulatory tripeptide
    • Roy S., Bayly C.I., Gareau Y., Houtzager V.M., Kargman S., Keen S.L., et al. Maintenance of caspase-3 proenzyme dormancy by an intrinsic "safety catch" regulatory tripeptide. Proc. Natl Acad. Sci. USA 98 (2001) 6132-6137
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6132-6137
    • Roy, S.1    Bayly, C.I.2    Gareau, Y.3    Houtzager, V.M.4    Kargman, S.5    Keen, S.L.6
  • 23
    • 11344295388 scopus 로고    scopus 로고
    • Analysis of pH-dependent elements in proteins: geometry and properties of pairs of hydrogen-bonded carboxylic acid side-chains
    • Gerd W. Analysis of pH-dependent elements in proteins: geometry and properties of pairs of hydrogen-bonded carboxylic acid side-chains. Proteins: Struct. Funct. Bioinformat. 58 (2005) 396-406
    • (2005) Proteins: Struct. Funct. Bioinformat. , vol.58 , pp. 396-406
    • Gerd, W.1
  • 24
    • 0030632978 scopus 로고    scopus 로고
    • "Strong" hydrogen bonds in chemistry and biology
    • Perrin C.L., and Nielson J.B. "Strong" hydrogen bonds in chemistry and biology. Annu. Rev. Phys. Chem. 48 (1997) 511-544
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 511-544
    • Perrin, C.L.1    Nielson, J.B.2
  • 27
    • 33644876080 scopus 로고    scopus 로고
    • Some aspects of quantitative analysis and correction of radiation damage
    • Diederichs K. Some aspects of quantitative analysis and correction of radiation damage. Acta Crystallog. sect. D 62 (2006) 96-101
    • (2006) Acta Crystallog. sect. D , vol.62 , pp. 96-101
    • Diederichs, K.1
  • 28
    • 10944256201 scopus 로고    scopus 로고
    • Ionic interactions near the 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. Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3. Biochem. J. 384 (2004) 515-525
    • (2004) Biochem. J. , vol.384 , pp. 515-525
    • Feeney, B.1    Pop, C.2    Tripathy, A.3    Clark, A.C.4
  • 31
    • 33745255559 scopus 로고    scopus 로고
    • Esther, D., Lenherr, B. A., Grutter, M. G. (2004). Kinetic characterization of caspase-8. Diploma thesis. Department of Biochemistry, University of Zurich (unpublished results).
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Cryst. D50 (1994) 760-763
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 37
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallog. 21 (1988) 67-72
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 67-72
    • Kabsch, W.1
  • 38
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21 (1988) 916-924
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 40
    • 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 41


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