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Volumn 10, Issue 11, 2002, Pages 1509-1519

Monomeric structures of the zymogen and active catalytic domain of complement protease C1r: Further insights into the C1 activation mechanism

Author keywords

Activation; Complement; Innate immunity; Serine protease; Substrate specificity

Indexed keywords

ENZYME PRECURSOR; PROTEINASE; PROTEINASE C1R; UNCLASSIFIED DRUG; COMPLEMENT COMPONENT C1R;

EID: 0036850943     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00881-X     Document Type: Article
Times cited : (51)

References (43)
  • 1
    • 0029987839 scopus 로고    scopus 로고
    • The instructive role of innate immunity in the acquired immune response
    • Fearon D.T., Locksley R.M. The instructive role of innate immunity in the acquired immune response. Science. 272:1996;50-54.
    • (1996) Science , vol.272 , pp. 50-54
    • Fearon, D.T.1    Locksley, R.M.2
  • 3
    • 0021894435 scopus 로고
    • The classical complement pathway: Activation and regulation of the first complement component
    • Cooper N.R. The classical complement pathway. activation and regulation of the first complement component Adv. Immunol. 37:1985;151-216.
    • (1985) Adv. Immunol. , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 4
    • 0023137465 scopus 로고
    • A functional model of the human C1 complex
    • Arlaud G.J., Colomb M.G., Gagnon J. A functional model of the human C1 complex. Immunol. Today. 8:1987;106-111.
    • (1987) Immunol. Today , vol.8 , pp. 106-111
    • Arlaud, G.J.1    Colomb, M.G.2    Gagnon, J.3
  • 6
    • 0033947551 scopus 로고    scopus 로고
    • C1q: Structure, function, and receptors
    • Kishore U., Reid K.B.M. C1q. structure, function, and receptors Immunopharmacology. 49:2000;159-170.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.M.2
  • 8
    • 0026526251 scopus 로고
    • The complement system in xenotransplantation
    • Dalmasso A.P. The complement system in xenotransplantation. Immunopharmacology. 24:1992;149-160.
    • (1992) Immunopharmacology , vol.24 , pp. 149-160
    • Dalmasso, A.P.1
  • 10
    • 0035575742 scopus 로고    scopus 로고
    • β-amyloid fibrils activate the C1 complex of complement under physiological conditions. Evidence for a binding site for A β on the C1q globular regions
    • Tacnet-Delorme P., Chevallier S., Arlaud G.J. β-amyloid fibrils activate the C1 complex of complement under physiological conditions. Evidence for a binding site for A β on the C1q globular regions. J. Immunol. 167:2001;6374-6381.
    • (2001) J. Immunol. , vol.167 , pp. 6374-6381
    • Tacnet-Delorme, P.1    Chevallier, S.2    Arlaud, G.J.3
  • 12
    • 0035053039 scopus 로고    scopus 로고
    • Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie
    • Mabbott N.A., Bruce M.E., Botto M., Walport M.J., Pepys M.B. Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie. Nat. Med. 7:2001;485-487.
    • (2001) Nat. Med. , vol.7 , pp. 485-487
    • Mabbott, N.A.1    Bruce, M.E.2    Botto, M.3    Walport, M.J.4    Pepys, M.B.5
  • 13
    • 0022557568 scopus 로고
    • A molecular mechanism for the activation of the first component of complement by immune complexes
    • Schumaker V.N., Hanson D.C., Kilchherr E., Phillips M.L., Poon P.H. A molecular mechanism for the activation of the first component of complement by immune complexes. Mol. Immunol. 23:1986;557-565.
    • (1986) Mol. Immunol. , vol.23 , pp. 557-565
    • Schumaker, V.N.1    Hanson, D.C.2    Kilchherr, E.3    Phillips, M.L.4    Poon, P.H.5
  • 14
    • 0023042319 scopus 로고
    • Functional model of subcomponent C1 of human complement
    • Weiss V., Fauser C., Engel J. Functional model of subcomponent C1 of human complement. J. Mol. Biol. 189:1986;573-581.
    • (1986) J. Mol. Biol. , vol.189 , pp. 573-581
    • Weiss, V.1    Fauser, C.2    Engel, J.3
  • 16
    • 0034678903 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human complement C1s: A serine protease with a handle
    • Gaboriaud C., Rossi V., Bally I., Arlaud G.J., Fontecilla-Camps J.C. Crystal structure of the catalytic domain of human complement C1s. a serine protease with a handle EMBO J. 19:2000;1755-1765.
    • (2000) EMBO J. , vol.19 , pp. 1755-1765
    • Gaboriaud, C.1    Rossi, V.2    Bally, I.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5
  • 17
    • 0036469280 scopus 로고    scopus 로고
    • The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
    • Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.C., Gaboriaud C. The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J. 21:2002;231-239.
    • (2002) EMBO J. , vol.21 , pp. 231-239
    • Budayova-Spano, M.1    Lacroix, M.2    Thielens, N.M.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5    Gaboriaud, C.6
  • 19
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • Perona J.J., Craik C.S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272:1997;29987-29990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 20
    • 0030802519 scopus 로고    scopus 로고
    • The co-crystal structure of unliganded bovine α-thrombin and prethrombin-2: Movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding
    • Malkowski M.G., Martin P.D., Guzik J.C., Edwards B.F. The co-crystal structure of unliganded bovine α-thrombin and prethrombin-2. movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding Protein Sci. 6:1997;1438-1448.
    • (1997) Protein Sci. , vol.6 , pp. 1438-1448
    • Malkowski, M.G.1    Martin, P.D.2    Guzik, J.C.3    Edwards, B.F.4
  • 21
    • 0030811924 scopus 로고    scopus 로고
    • Comparative analysis of haemostatic proteinases: Structural aspects of thrombin, factor Xa, factor IXa and protein C
    • Bode W., Brandstetter H., Mather T., Stubbs M.T. Comparative analysis of haemostatic proteinases. structural aspects of thrombin, factor Xa, factor IXa and protein C Thromb. Haemost. 78:1997;501-511.
    • (1997) Thromb. Haemost. , vol.78 , pp. 501-511
    • Bode, W.1    Brandstetter, H.2    Mather, T.3    Stubbs, M.T.4
  • 22
    • 0033557766 scopus 로고    scopus 로고
    • Structural basis of profactor D activation: From a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
    • Jing H., Macon K.J., Moore D., DeLucas L.J., Volanakis J.E., Narayana S.V. Structural basis of profactor D activation. from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D EMBO J. 18:1999;804-814.
    • (1999) EMBO J. , vol.18 , pp. 804-814
    • Jing, H.1    Macon, K.J.2    Moore, D.3    DeLucas, L.J.4    Volanakis, J.E.5    Narayana, S.V.6
  • 23
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204:1992;433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 25
    • 0029785840 scopus 로고    scopus 로고
    • +-induced allosteric regulation of catalytic activity in serine proteases
    • +-induced allosteric regulation of catalytic activity in serine proteases. Proc. Natl. Acad. Sci. USA. 93:1996;10653-10656.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10653-10656
    • Dang, Q.D.1    Di Cera, E.2
  • 28
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R., Bode W. Structural basis of the activation and action of trypsin. J. Am. Chem. Soc. 11:1978;114-122.
    • (1978) J. Am. Chem. Soc. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 29
    • 0014965896 scopus 로고
    • Chymotrypsinogen: 2.5 Å crystal structure, comparison with α-chymotrypsin and implications for zymogen activation
    • Freer S.T., Kraut J., Robertus J.D., Wright H.T., Xuong N.H. Chymotrypsinogen. 2.5 Å crystal structure, comparison with α-chymotrypsin and implications for zymogen activation Biochemistry. 11:1970;1997-2009.
    • (1970) Biochemistry , vol.11 , pp. 1997-2009
    • Freer, S.T.1    Kraut, J.2    Robertus, J.D.3    Wright, H.T.4    Xuong, N.H.5
  • 30
    • 0034723145 scopus 로고    scopus 로고
    • Human plasminogen catalytic domain undergoes an unusual conformational change upon activation
    • Wang X., Terzyan S., Tang J., Loy J.A., Lin X., Zhang X.C. Human plasminogen catalytic domain undergoes an unusual conformational change upon activation. J. Mol. Biol. 295:2000;903-914.
    • (2000) J. Mol. Biol. , vol.295 , pp. 903-914
    • Wang, X.1    Terzyan, S.2    Tang, J.3    Loy, J.A.4    Lin, X.5    Zhang, X.C.6
  • 32
    • 0002414103 scopus 로고
    • Molecular data processing
    • D. Moras, A.D. Podjarny, & J.C. Thierry. Oxford: Oxford University Press
    • Leslie A.G.W. Molecular data processing. Moras D., Podjarny A.D., Thierry J.C. Crystallographic Computing. 1991;Oxford University Press, Oxford. 50-61.pp.
    • (1991) Crystallographic Computing , pp. 50-61
    • Leslie, A.G.W.1
  • 33
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 34
    • 0034761713 scopus 로고    scopus 로고
    • Automated data processing on beamline FIP (BM30A) at ESRF
    • Ferrer J.-L. Automated data processing on beamline FIP (BM30A) at ESRF. Acta Crystallogr. D. 57:2001;1752-1753.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1752-1753
    • Ferrer, J.-L.1
  • 35
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 36
    • 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., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing accuracy of crystal structures
    • Brünger A.T. Free R value. a novel statistical quantity for assessing accuracy of crystal structures Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 40
    • 0011465585 scopus 로고    scopus 로고
    • NACCESS Computer Program, Department of Biochemistry and Molecular Biology, University College London, UK
    • Hubbard, S.J., and Thornton, J.M. (1993). NACCESS Computer Program, Department of Biochemistry and Molecular Biology, University College London, UK.
    • Hubbard, S.J.1    Thornton, J.M.2
  • 41
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 43
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.