메뉴 건너뛰기




Volumn 380, Issue 2, 2008, Pages 351-360

Structure of an Fab-Protease Complex Reveals a Highly Specific Non-canonical Mechanism of Inhibition

Author keywords

antibody; protease inhibitor; serine protease; structure; substrate specificity

Indexed keywords

FAB ANTIBODY INHIBITOR; MATRIPTASE; PROTEINASE INHIBITOR;

EID: 44949119318     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.009     Document Type: Article
Times cited : (52)

References (46)
  • 2
    • 0035914320 scopus 로고    scopus 로고
    • Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity
    • Roussel A., Mathieu M., Dobbs A., Luu B., Cambillau C., and Kellenberger C. Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity. J. Biol. Chem. 276 (2001) 38893-38898
    • (2001) J. Biol. Chem. , vol.276 , pp. 38893-38898
    • Roussel, A.1    Mathieu, M.2    Dobbs, A.3    Luu, B.4    Cambillau, C.5    Kellenberger, C.6
  • 3
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens L.M., Fingleton B., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295 (2002) 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 4
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nature Rev. Drug Discov. 5 (2006) 785-799
    • (2006) Nature Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 6
    • 33646160613 scopus 로고    scopus 로고
    • Microinjection of an antibody against the cysteine-protease involved in male chromatin remodeling blocks the development of sea urchin embryos at the initial cell cycle
    • Puchi M., Quinones K., Concha C., Iribarren C., Bustos P., Morin V., et al. Microinjection of an antibody against the cysteine-protease involved in male chromatin remodeling blocks the development of sea urchin embryos at the initial cell cycle. J. Cell Biochem. 98 (2006) 335-342
    • (2006) J. Cell Biochem. , vol.98 , pp. 335-342
    • Puchi, M.1    Quinones, K.2    Concha, C.3    Iribarren, C.4    Bustos, P.5    Morin, V.6
  • 7
    • 33644500443 scopus 로고    scopus 로고
    • The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH
    • Fukuoka Y., and Schwartz L.B. The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH. J. Immunol. 176 (2006) 3165-3172
    • (2006) J. Immunol. , vol.176 , pp. 3165-3172
    • Fukuoka, Y.1    Schwartz, L.B.2
  • 8
    • 18544367029 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase is involved in migration of human monocytes and is regulated through their interaction with fibronectin or endothelium
    • Matias-Roman S., Galvez B.G., Genis L., Yanez-Mo M., de la Rosa G., Sanchez-Mateos P., et al. Membrane type 1-matrix metalloproteinase is involved in migration of human monocytes and is regulated through their interaction with fibronectin or endothelium. Blood 105 (2005) 3956-3964
    • (2005) Blood , vol.105 , pp. 3956-3964
    • Matias-Roman, S.1    Galvez, B.G.2    Genis, L.3    Yanez-Mo, M.4    de la Rosa, G.5    Sanchez-Mateos, P.6
  • 9
    • 0034832988 scopus 로고    scopus 로고
    • Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme
    • Petersen H.H., Hansen M., Schousboe S.L., and Andreasen P.A. Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme. Eur. J. Biochem. 268 (2001) 4430-4439
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4430-4439
    • Petersen, H.H.1    Hansen, M.2    Schousboe, S.L.3    Andreasen, P.A.4
  • 10
    • 33645748575 scopus 로고    scopus 로고
    • Antibodies neutralizing hepsin protease activity do not impact cell growth but inhibit invasion of prostate and ovarian tumor cells in culture
    • Xuan J.A., Schneider D., Toy P., Lin R., Newton A., Zhu Y., et al. Antibodies neutralizing hepsin protease activity do not impact cell growth but inhibit invasion of prostate and ovarian tumor cells in culture. Cancer Res. 66 (2006) 3611-3619
    • (2006) Cancer Res. , vol.66 , pp. 3611-3619
    • Xuan, J.A.1    Schneider, D.2    Toy, P.3    Lin, R.4    Newton, A.5    Zhu, Y.6
  • 11
    • 33745824230 scopus 로고    scopus 로고
    • Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells
    • Obermajer N., Premzl A., Zavasnik Bergant T., Turk B., and Kos J. Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells. Expt. Cell Res. 312 (2006) 2515-2527
    • (2006) Expt. Cell Res. , vol.312 , pp. 2515-2527
    • Obermajer, N.1    Premzl, A.2    Zavasnik Bergant, T.3    Turk, B.4    Kos, J.5
  • 12
    • 0037417780 scopus 로고    scopus 로고
    • Potent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies
    • Sun J., Pons J., and Craik C.S. Potent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies. Biochemistry 42 (2003) 892-900
    • (2003) Biochemistry , vol.42 , pp. 892-900
    • Sun, J.1    Pons, J.2    Craik, C.S.3
  • 13
    • 34248583079 scopus 로고    scopus 로고
    • The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1)
    • Farady C.J., Sun J., Darragh M.R., Miller S.M., and Craik C.S. The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1). J. Mol. Biol. 369 (2007) 1041-1051
    • (2007) J. Mol. Biol. , vol.369 , pp. 1041-1051
    • Farady, C.J.1    Sun, J.2    Darragh, M.R.3    Miller, S.M.4    Craik, C.S.5
  • 14
    • 23944489424 scopus 로고    scopus 로고
    • Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation
    • List K., Szabo R., Molinolo A., Sriuranpong V., Redeye V., Murdock T., et al. Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation. Genes Dev. 19 (2005) 1934-1950
    • (2005) Genes Dev. , vol.19 , pp. 1934-1950
    • List, K.1    Szabo, R.2    Molinolo, A.3    Sriuranpong, V.4    Redeye, V.5    Murdock, T.6
  • 15
    • 34248535705 scopus 로고    scopus 로고
    • Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway
    • Bhatt A.S., Welm A., Farady C.J., Vasquez M., Wilson K., and Craik C.S. Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway. Proc. Natl Acad. Sci. USA 104 (2007) 5771-5776
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5771-5776
    • Bhatt, A.S.1    Welm, A.2    Farady, C.J.3    Vasquez, M.4    Wilson, K.5    Craik, C.S.6
  • 16
    • 34250653300 scopus 로고    scopus 로고
    • The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans
    • Welm A.L., Sneddon J.B., Taylor C., Nuyten D.S., van de Vijver M.J., Hasegawa B.H., and Bishop J.M. The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans. Proc. Natl Acad. Sci. USA 104 (2007) 7570-7575
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 7570-7575
    • Welm, A.L.1    Sneddon, J.B.2    Taylor, C.3    Nuyten, D.S.4    van de Vijver, M.J.5    Hasegawa, B.H.6    Bishop, J.M.7
  • 17
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A., Ge L., Honegger A., Pack P., Fischer M., Wellnhofer G., et al. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296 (2000) 57-86
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6
  • 18
    • 0033603596 scopus 로고    scopus 로고
    • A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies
    • de Haard H.J., van Neer N., Reurs A., Hufton S.E., Roovers R.C., Henderikx P., et al. A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies. J. Biol. Chem. 274 (1999) 18218-18230
    • (1999) J. Biol. Chem. , vol.274 , pp. 18218-18230
    • de Haard, H.J.1    van Neer, N.2    Reurs, A.3    Hufton, S.E.4    Roovers, R.C.5    Henderikx, P.6
  • 19
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • Perona J.J., and 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
    • 0037127319 scopus 로고    scopus 로고
    • Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase
    • Friedrich R., Fuentes-Prior P., Ong E., Coombs G., Hunter M., Oehler R., et al. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J. Biol. Chem. 277 (2002) 2160-2168
    • (2002) J. Biol. Chem. , vol.277 , pp. 2160-2168
    • Friedrich, R.1    Fuentes-Prior, P.2    Ong, E.3    Coombs, G.4    Hunter, M.5    Oehler, R.6
  • 22
    • 0015919469 scopus 로고
    • Detailed mechanism of interaction of bovine -trypsin with soybean trypsin inhibitor (Kunitz). I. Stopped flow measurements
    • Luthy J.A., Praissman M., Finkenstadt W.R., and Laskowski Jr. M. Detailed mechanism of interaction of bovine -trypsin with soybean trypsin inhibitor (Kunitz). I. Stopped flow measurements. J. Biol. Chem. 248 (1973) 1760-1771
    • (1973) J. Biol. Chem. , vol.248 , pp. 1760-1771
    • Luthy, J.A.1    Praissman, M.2    Finkenstadt, W.R.3    Laskowski Jr., M.4
  • 23
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution
    • Bode W., Schwager P., and Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution. J. Mol. Biol. 118 (1978) 99-112
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 24
    • 0002770758 scopus 로고
    • Biochemistry of aprotinin and aprotinin-like inhibitors
    • Barrett A.J., and Salvesen G. (Eds), Elsevier, New York
    • Gebhard W., Tschesche T., and Fritz H. Biochemistry of aprotinin and aprotinin-like inhibitors. In: Barrett A.J., and Salvesen G. (Eds). Proteinase Inhibitors (1986), Elsevier, New York 55-152
    • (1986) Proteinase Inhibitors , pp. 55-152
    • Gebhard, W.1    Tschesche, T.2    Fritz, H.3
  • 25
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., and Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234 (1993) 946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 26
    • 0032488808 scopus 로고    scopus 로고
    • The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF.G9 complex
    • Huang M., Syed R., Stura E.A., Stone M.J., Stefanko R.S., Ruf W., et al. The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF.G9 complex. J. Mol. Biol. 275 (1998) 873-894
    • (1998) J. Mol. Biol. , vol.275 , pp. 873-894
    • Huang, M.1    Syed, R.2    Stura, E.A.3    Stone, M.J.4    Stefanko, R.S.5    Ruf, W.6
  • 27
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 28
    • 33846675236 scopus 로고    scopus 로고
    • Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2
    • Maskos K., Lang R., Tschesche H., and Bode W. Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2. J. Mol. Biol. 366 (2007) 1222-1231
    • (2007) J. Mol. Biol. , vol.366 , pp. 1222-1231
    • Maskos, K.1    Lang, R.2    Tschesche, H.3    Bode, W.4
  • 29
    • 0037459045 scopus 로고    scopus 로고
    • Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
    • Jenko S., Dolenc I., Guncar G., Dobersek A., Podobnik M., and Turk D. Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J. Mol. Biol. 326 (2003) 875-885
    • (2003) J. Mol. Biol. , vol.326 , pp. 875-885
    • Jenko, S.1    Dolenc, I.2    Guncar, G.3    Dobersek, A.4    Podobnik, M.5    Turk, D.6
  • 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., and 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 Sci. 6 (1997) 1806-1824
    • (1997) Protein Sci. , 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
    • 0028100458 scopus 로고
    • Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection
    • Dennis M.S., and Lazarus R.A. Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection. J. Biol. Chem. 269 (1994) 22137-22144
    • (1994) J. Biol. Chem. , vol.269 , pp. 22137-22144
    • Dennis, M.S.1    Lazarus, R.A.2
  • 33
    • 0141815667 scopus 로고    scopus 로고
    • Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1
    • Kirchhofer D., Peek M., Li W., Stamos J., Eigenbrot C., Kadkhodayan S., et al. Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1. J. Biol. Chem. 278 (2003) 36341-36349
    • (2003) J. Biol. Chem. , vol.278 , pp. 36341-36349
    • Kirchhofer, D.1    Peek, M.2    Li, W.3    Stamos, J.4    Eigenbrot, C.5    Kadkhodayan, S.6
  • 34
    • 0042861481 scopus 로고    scopus 로고
    • Engineering of a macromolecular scaffold to develop specific protease inhibitors
    • Stoop A.A., and Craik C.S. Engineering of a macromolecular scaffold to develop specific protease inhibitors. Nature Biotechnol. 21 (2003) 1063-1068
    • (2003) Nature Biotechnol. , vol.21 , pp. 1063-1068
    • Stoop, A.A.1    Craik, C.S.2
  • 35
    • 37849023521 scopus 로고    scopus 로고
    • Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1
    • Li P., Jiang S., Lee S.L., Lin C.Y., Johnson M.D., Dickson R.B., et al. Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1. J. Med. Chem. 50 (2007) 5976-5983
    • (2007) J. Med. Chem. , vol.50 , pp. 5976-5983
    • Li, P.1    Jiang, S.2    Lee, S.L.3    Lin, C.Y.4    Johnson, M.D.5    Dickson, R.B.6
  • 36
    • 34548642972 scopus 로고    scopus 로고
    • Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1
    • Zhao G., Yuan C., Wind T., Huang Z., Andreasen P.A., and Huang M. Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1. J. Struct. Biol. 160 (2007) 1-10
    • (2007) J. Struct. Biol. , vol.160 , pp. 1-10
    • Zhao, G.1    Yuan, C.2    Wind, T.3    Huang, Z.4    Andreasen, P.A.5    Huang, M.6
  • 37
    • 38049174343 scopus 로고    scopus 로고
    • Structural insight into distinct mechanisms of protease inhibition by antibodies
    • Wu Y., Eigenbrot C., Liang W.-C., Stawicki S., Shia S., Fan B., et al. Structural insight into distinct mechanisms of protease inhibition by antibodies. Proc. Natl Acad. Sci. USA 104 (2007) 19784-19789
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19784-19789
    • Wu, Y.1    Eigenbrot, C.2    Liang, W.-C.3    Stawicki, S.4    Shia, S.5    Fan, B.6
  • 38
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • Takeuchi T., Shuman M.A., and Craik C.S. Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc. Natl Acad. Sci. USA 96 (1999) 11054-11061
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 39
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 40
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams J.W., and Morrison J.F. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63 (1979) 437-467
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 41
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • Holton J., and Alber T. Automated protein crystal structure determination using ELVES. Proc. Natl Acad. Sci. USA 101 (2004) 1537-1542
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 42
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D 57 (2001) 1373-1382
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 43
    • 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 Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.