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Volumn 6, Issue , 2016, Pages

The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers

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EID: 84989193408     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep34303     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol 3, 753-766 (2002).
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 3
    • 84881238159 scopus 로고    scopus 로고
    • The multifaceted proprotein convertases: Their unique, redundant, complementary, and opposite functions
    • Seidah, N. G, Sadr, M. S, Chretien, M. & Mbikay, M. The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions. J Biol Chem 288, 21473-21481 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 21473-21481
    • Seidah, N.G.1    Sadr, M.S.2    Chretien, M.3    Mbikay, M.4
  • 4
    • 0037743535 scopus 로고    scopus 로고
    • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
    • Henrich, S. et al. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat Struct Biol 10, 520-526 (2003).
    • (2003) Nat Struct Biol , vol.10 , pp. 520-526
    • Henrich, S.1
  • 6
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah, N. G. & Prat, A. The biology and therapeutic targeting of the proprotein convertases. Nat Rev Drug Discov 11, 367-383 (2012).
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 7
    • 27744541223 scopus 로고    scopus 로고
    • Inhibitors of proprotein convertases
    • Basak, A. Inhibitors of proprotein convertases. J Mol Med 83, 844-855 (2005).
    • (2005) J Mol Med , vol.83 , pp. 844-855
    • Basak, A.1
  • 8
    • 41649118952 scopus 로고    scopus 로고
    • A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness
    • Coppola, J. M, Bhojani, M. S, Ross, B. D. & Rehemtulla, A. A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness. Neoplasia 10, 363-370 (2008).
    • (2008) Neoplasia , vol.10 , pp. 363-370
    • Coppola, J.M.1    Bhojani, M.S.2    Ross, B.D.3    Rehemtulla, A.4
  • 9
    • 20144371230 scopus 로고    scopus 로고
    • Human carcinoma cell growth and invasiveness is impaired by the propeptide of the ubiquitous proprotein convertase furin
    • Lopez de Cicco, R, Bassi, D. E, Zucker, S, Seidah, N. G. & Klein-Szanto, A. J. Human carcinoma cell growth and invasiveness is impaired by the propeptide of the ubiquitous proprotein convertase furin. Cancer research 65, 4162-4171 (2005).
    • (2005) Cancer Research , vol.65 , pp. 4162-4171
    • Lopez De Cicco, R.1    Bassi, D.E.2    Zucker, S.3    Seidah, N.G.4    Klein-Szanto, A.J.5
  • 10
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger, S, Bosch, V, Angliker, H, Shaw, E, Klenk, H. D. & Garten, W. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360, 358-361 (1992).
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 11
    • 84933502451 scopus 로고    scopus 로고
    • Novel Furin Inhibitors with Potent Anti-infectious Activity
    • Hardes, K. et al. Novel Furin Inhibitors with Potent Anti-infectious Activity. ChemMedChem (2015).
    • (2015) ChemMedChem
    • Hardes, K.1
  • 12
    • 84860380797 scopus 로고    scopus 로고
    • On the cutting edge of proprotein convertase pharmacology: From molecular concepts to clinical applications
    • Couture, F, D'Anjou, F. & Day, R. On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications. Biomolecular concepts 2, 421-438 (2011).
    • (2011) Biomolecular Concepts , vol.2 , pp. 421-438
    • Couture, F.1    D'Anjou, F.2    Day, R.3
  • 13
    • 9644281041 scopus 로고    scopus 로고
    • Proprotein convertase models based on the crystal structures of furin and kexin: Explanation of their specificity
    • Henrich, S, Lindberg, I, Bode, W. & Than, M. E. Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J Mol Biol 345, 211-227 (2005).
    • (2005) J Mol Biol , vol.345 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 14
    • 84934890156 scopus 로고    scopus 로고
    • Peptidomimetic furin inhibitor MI-701 in combination with oseltamivir and ribavirin efficiently blocks propagation of highly pathogenic avian influenza viruses and delays high level oseltamivir resistance in MDCK cells
    • Lu, Y. et al. Peptidomimetic furin inhibitor MI-701 in combination with oseltamivir and ribavirin efficiently blocks propagation of highly pathogenic avian influenza viruses and delays high level oseltamivir resistance in MDCK cells. Antiviral Res 120, 89-100 (2015).
    • (2015) Antiviral Res , vol.120 , pp. 89-100
    • Lu, Y.1
  • 16
    • 1542297713 scopus 로고    scopus 로고
    • Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases
    • Holyoak, T, Kettner, C. A, Petsko, G. A, Fuller, R. S. & Ringe, D. Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases. Biochemistry 43, 2412-2421 (2004).
    • (2004) Biochemistry , vol.43 , pp. 2412-2421
    • Holyoak, T.1    Kettner, C.A.2    Petsko, G.A.3    Fuller, R.S.4    Ringe, D.5
  • 17
    • 34249848612 scopus 로고    scopus 로고
    • Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2
    • Wheatley, J. L. & Holyoak, T. Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2. Proc Natl Acad Sci USA 104, 6626-6631 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6626-6631
    • Wheatley, J.L.1    Holyoak, T.2
  • 18
    • 77956700490 scopus 로고    scopus 로고
    • Structural and mechanistic insight into how antibodies inhibit serine proteases
    • Ganesan, R, Eigenbrot, C. & Kirchhofer, D. Structural and mechanistic insight into how antibodies inhibit serine proteases. Biochem J 430, 179-189 (2010).
    • (2010) Biochem J , vol.430 , pp. 179-189
    • Ganesan, R.1    Eigenbrot, C.2    Kirchhofer, D.3
  • 19
    • 38049174343 scopus 로고    scopus 로고
    • Structural insight into distinct mechanisms of protease inhibition by antibodies
    • Wu, Y. et al. Structural insight into distinct mechanisms of protease inhibition by antibodies. Proc Natl Acad Sci USA 104, 19784-19789 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19784-19789
    • Wu, Y.1
  • 20
    • 44949119318 scopus 로고    scopus 로고
    • Structure of an Fab-protease complex reveals a highly specific non-canonical mechanism of inhibition
    • Farady, C. J, Egea, P. F, Schneider, E. L, Darragh, M. R. & Craik, C. S. Structure of an Fab-protease complex reveals a highly specific non-canonical mechanism of inhibition. J Mol Biol 380, 351-360 (2008).
    • (2008) J Mol Biol , vol.380 , pp. 351-360
    • Farady, C.J.1    Egea, P.F.2    Schneider, E.L.3    Darragh, M.R.4    Craik, C.S.5
  • 21
    • 79955014374 scopus 로고    scopus 로고
    • Cross-domain inhibition of TACE ectodomain
    • Tape, C. J. et al. Cross-domain inhibition of TACE ectodomain. Proc Natl Acad Sci USA 108, 5578-5583 (2011).
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5578-5583
    • Tape, C.J.1
  • 22
    • 84955478819 scopus 로고    scopus 로고
    • The trimeric serine protease HtrA1 forms a cage-like inhibition complex with an anti-HtrA1 antibody
    • Ciferri, C. et al. The trimeric serine protease HtrA1 forms a cage-like inhibition complex with an anti-HtrA1 antibody. Biochem J 472, 169-181 (2015).
    • (2015) Biochem J , vol.472 , pp. 169-181
    • Ciferri, C.1
  • 24
    • 84857841703 scopus 로고    scopus 로고
    • Allosteric antibody inhibition of human hepsin protease
    • Koschubs, T. et al. Allosteric antibody inhibition of human hepsin protease. Biochem J 442, 483-494 (2012).
    • (2012) Biochem J , vol.442 , pp. 483-494
    • Koschubs, T.1
  • 25
    • 71049189254 scopus 로고    scopus 로고
    • Unraveling the allosteric mechanism of serine protease inhibition by an antibody
    • Ganesan, R. et al. Unraveling the allosteric mechanism of serine protease inhibition by an antibody. Structure 17, 1614-1624 (2009).
    • (2009) Structure , vol.17 , pp. 1614-1624
    • Ganesan, R.1
  • 26
    • 79952009210 scopus 로고    scopus 로고
    • Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition
    • Oyen, D, Srinivasan, V, Steyaert, J. & Barlow, J. N. Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition. J Mol Biol 407, 138-148 (2011).
    • (2011) J Mol Biol , vol.407 , pp. 138-148
    • Oyen, D.1    Srinivasan, V.2    Steyaert, J.3    Barlow, J.N.4
  • 27
    • 84867762574 scopus 로고    scopus 로고
    • Generation and characterization of non-competitive furin-inhibiting nanobodies
    • Zhu, J. et al. Generation and characterization of non-competitive furin-inhibiting nanobodies. Biochem J 448, 73-82 (2012).
    • (2012) Biochem J , vol.448 , pp. 73-82
    • Zhu, J.1
  • 28
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. & Henrick, K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60, 2256-2268 (2004).
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 30
    • 0030794907 scopus 로고    scopus 로고
    • Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities
    • Scheidig, A. J, Hynes, T. R, Pelletier, L. A, Wells, J. A. & Kossiakoff, A. A. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities. Protein science: a publication of the Protein Society 6, 1806-1824 (1997).
    • (1997) Protein Science: A Publication of the Protein Society , vol.6 , pp. 1806-1824
    • Scheidig, A.J.1    Hynes, T.R.2    Pelletier, L.A.3    Wells, J.A.4    Kossiakoff, A.A.5
  • 31
    • 84883257823 scopus 로고    scopus 로고
    • The activation peptide of coagulation factor IX and X serves as a high affinity receptor to cationic ligands
    • Griessner, A, Zögg, T. & Brandstetter, H. The activation peptide of coagulation factor IX and X serves as a high affinity receptor to cationic ligands. Thrombosis and Haemostasis 110, 620-622 (2013).
    • (2013) Thrombosis and Haemostasis , vol.110 , pp. 620-622
    • Griessner, A.1    Zögg, T.2    Brandstetter, H.3
  • 32
    • 0037423301 scopus 로고    scopus 로고
    • Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop
    • Sichler, K, Kopetzki, E, Huber, R, Bode, W, Hopfner, K. P. & Brandstetter, H. Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop. J Biol Chem 278, 4121-4126 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 4121-4126
    • Sichler, K.1    Kopetzki, E.2    Huber, R.3    Bode, W.4    Hopfner, K.P.5    Brandstetter, H.6
  • 33
    • 33646581724 scopus 로고    scopus 로고
    • Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
    • Johnson, D. J, Li, W, Adams, T. E. & Huntington, J. A. Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. The EMBO journal 25, 2029-2037 (2006).
    • (2006) The EMBO Journal , vol.25 , pp. 2029-2037
    • Johnson, D.J.1    Li, W.2    Adams, T.E.3    Huntington, J.A.4
  • 34
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: The power of in vitro display technologies
    • Bradbury, A. R, Sidhu, S, Dubel, S. & McCafferty, J. Beyond natural antibodies: the power of in vitro display technologies. Nature biotechnology 29, 245-254 (2011).
    • (2011) Nature Biotechnology , vol.29 , pp. 245-254
    • Bradbury, A.R.1    Sidhu, S.2    Dubel, S.3    McCafferty, J.4
  • 35
    • 84860129612 scopus 로고    scopus 로고
    • Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin
    • Mueller, U. et al. Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin. Journal of synchrotron radiation 19, 442-449 (2012).
    • (2012) Journal of Synchrotron Radiation , vol.19 , pp. 442-449
    • Mueller, U.1
  • 37
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67, 235-242 (2011).
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 40
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213-221 (2010).
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 41
    • 84881304302 scopus 로고    scopus 로고
    • MAIN software for density averaging, model building, structure refinement and validation
    • Turk, D. MAIN software for density averaging, model building, structure refinement and validation. Acta Crystallogr D Biol Crystallogr 69, 1342-1357 (2013).
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 1342-1357
    • Turk, D.1


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