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Volumn 22, Issue 9, 2014, Pages 1333-1340

Structures of neutrophil serine protease 4 reveal an unusual mechanism of substrate recognition by a trypsin-fold protease

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ELASTASE; NEUTROPHIL SERINE PROTEINASE 4; SERINE PROTEINASE; TRYPSIN FOLD PROTEASE; UNCLASSIFIED DRUG; NSP4 SERINE PROTEASE; PROTEIN BINDING;

EID: 84930065206     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.07.008     Document Type: Article
Times cited : (20)

References (50)
  • 2
    • 0015220520 scopus 로고
    • Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin
    • G.S. Baldwin, and P.R. Carnegie Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin Science 171 1971 579 581
    • (1971) Science , vol.171 , pp. 579-581
    • Baldwin, G.S.1    Carnegie, P.R.2
  • 3
    • 84880449571 scopus 로고    scopus 로고
    • SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G
    • S1-S6
    • M. Baumann, C.T.N. Pham, and C. Benarafa SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G Blood 121 2013 3900 3907 S1-S6
    • (2013) Blood , vol.121 , pp. 3900-3907
    • Baumann, M.1    Pham, C.T.N.2    Benarafa, C.3
  • 4
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • M.T. Bedford, and S.G. Clarke Protein arginine methylation in mammals: who, what, and why Mol. Cell 33 2009 1 13
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 5
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • A. Belaaouaj, R. McCarthy, M. Baumann, Z. Gao, T.J. Ley, S.N. Abraham, and S.D. Shapiro Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis Nat. Med. 4 1998 615 618
    • (1998) Nat. Med. , vol.4 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6    Shapiro, S.D.7
  • 7
    • 10744220468 scopus 로고    scopus 로고
    • The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: A bioinformatics assessment
    • H.F. Clark, A.L. Gurney, E. Abaya, K. Baker, D. Baldwin, J. Brush, J. Chen, B. Chow, C. Chui, and C. Crowley et al. The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment Genome Res. 13 2003 2265 2270
    • (2003) Genome Res. , vol.13 , pp. 2265-2270
    • Clark, H.F.1    Gurney, A.L.2    Abaya, E.3    Baker, K.4    Baldwin, D.5    Brush, J.6    Chen, J.7    Chow, B.8    Chui, C.9    Crowley, C.10
  • 8
    • 0035951076 scopus 로고    scopus 로고
    • The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites
    • J. Cooley, T.K. Takayama, S.D. Shapiro, N.M. Schechter, and E. Remold-O'Donnell The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites Biochemistry 40 2001 15762 15770
    • (2001) Biochemistry , vol.40 , pp. 15762-15770
    • Cooley, J.1    Takayama, T.K.2    Shapiro, S.D.3    Schechter, N.M.4    Remold-O'Donnell, E.5
  • 10
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
    • Q. Deng, and J.T. Barbieri Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins Annu. Rev. Microbiol. 62 2008 271 288
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 11
    • 79961043508 scopus 로고    scopus 로고
    • Protein arginine methylation in parasitic protozoa
    • J.C. Fisk, and L.K. Read Protein arginine methylation in parasitic protozoa Eukaryot. Cell 10 2011 1013 1022
    • (2011) Eukaryot. Cell , vol.10 , pp. 1013-1022
    • Fisk, J.C.1    Read, L.K.2
  • 13
    • 0029833222 scopus 로고    scopus 로고
    • The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies
    • M. Fujinaga, M.M. Chernaia, R. Halenbeck, K. Koths, and M.N. James The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies J. Mol. Biol. 261 1996 267 278
    • (1996) J. Mol. Biol. , vol.261 , pp. 267-278
    • Fujinaga, M.1    Chernaia, M.M.2    Halenbeck, R.3    Koths, K.4    James, M.N.5
  • 16
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • L. Hedstrom Serine protease mechanism and specificity Chem. Rev. 102 2002 4501 4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 17
    • 0029853820 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: A Janus-faced proteinase with two opposite specificities
    • P. Hof, I. Mayr, R. Huber, E. Korzus, J. Potempa, J. Travis, J.C. Powers, and W. Bode The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities EMBO J. 15 1996 5481 5491
    • (1996) EMBO J. , vol.15 , pp. 5481-5491
    • Hof, P.1    Mayr, I.2    Huber, R.3    Korzus, E.4    Potempa, J.5    Travis, J.6    Powers, J.C.7    Bode, W.8
  • 20
    • 81455131876 scopus 로고    scopus 로고
    • Serglycin: A structural and functional chameleon with wide impact on immune cells
    • S.O. Kolset, and G. Pejler Serglycin: a structural and functional chameleon with wide impact on immune cells J. Immunol. 187 2011 4927 4933
    • (2011) J. Immunol. , vol.187 , pp. 4927-4933
    • Kolset, S.O.1    Pejler, G.2
  • 21
    • 78650096176 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases
    • B. Korkmaz, M.S. Horwitz, D.E. Jenne, and F. Gauthier Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases Pharmacol. Rev. 62 2010 726 759
    • (2010) Pharmacol. Rev. , vol.62 , pp. 726-759
    • Korkmaz, B.1    Horwitz, M.S.2    Jenne, D.E.3    Gauthier, F.4
  • 22
    • 0345708448 scopus 로고    scopus 로고
    • Neutrophil elastase cleaves PML-RARalpha and is important for the development of acute promyelocytic leukemia in mice
    • A.A. Lane, and T.J. Ley Neutrophil elastase cleaves PML-RARalpha and is important for the development of acute promyelocytic leukemia in mice Cell 115 2003 305 318
    • (2003) Cell , vol.115 , pp. 305-318
    • Lane, A.A.1    Ley, T.J.2
  • 23
    • 53449087927 scopus 로고    scopus 로고
    • Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: A naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
    • T. Loos, A. Mortier, M. Gouwy, I. Ronsse, W. Put, J.-P. Lenaerts, J. Van Damme, and P. Proost Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation Blood 112 2008 2648 2656
    • (2008) Blood , vol.112 , pp. 2648-2656
    • Loos, T.1    Mortier, A.2    Gouwy, M.3    Ronsse, I.4    Put, W.5    Lenaerts, J.-P.6    Van Damme, J.7    Proost, P.8
  • 24
    • 84879552493 scopus 로고    scopus 로고
    • Effect of Porphyromonas gingivalis on citrullination of proteins by macrophages in vitro
    • C. Marchant, M.D. Smith, S. Proudman, D.R. Haynes, and P.M. Bartold Effect of Porphyromonas gingivalis on citrullination of proteins by macrophages in vitro J. Periodontol. 84 2013 1272 1280
    • (2013) J. Periodontol. , vol.84 , pp. 1272-1280
    • Marchant, C.1    Smith, M.D.2    Proudman, S.3    Haynes, D.R.4    Bartold, P.M.5
  • 26
    • 77956899749 scopus 로고    scopus 로고
    • Posttranslational modification of the NH2-terminal region of CXCL5 by proteases or peptidylarginine deiminases (PAD) differently affects its biological activity
    • A. Mortier, T. Loos, M. Gouwy, I. Ronsse, J. Van Damme, and P. Proost Posttranslational modification of the NH2-terminal region of CXCL5 by proteases or peptidylarginine deiminases (PAD) differently affects its biological activity J. Biol. Chem. 285 2010 29750 29759
    • (2010) J. Biol. Chem. , vol.285 , pp. 29750-29759
    • Mortier, A.1    Loos, T.2    Gouwy, M.3    Ronsse, I.4    Van Damme, J.5    Proost, P.6
  • 28
    • 84884477446 scopus 로고    scopus 로고
    • Global substrate profiling of proteases in human neutrophil extracellular traps reveals consensus motif predominantly contributed by elastase
    • A.J. O'Donoghue, Y. Jin, G.M. Knudsen, N.C. Perera, D.E. Jenne, J.E. Murphy, C.S. Craik, and T.W. Hermiston Global substrate profiling of proteases in human neutrophil extracellular traps reveals consensus motif predominantly contributed by elastase PLoS ONE 8 2013 e75141
    • (2013) PLoS ONE , vol.8 , pp. 75141
    • O'Donoghue, A.J.1    Jin, Y.2    Knudsen, G.M.3    Perera, N.C.4    Jenne, D.E.5    Murphy, J.E.6    Craik, C.S.7    Hermiston, T.W.8
  • 30
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • V. Papayannopoulos, K.D. Metzler, A. Hakkim, and A. Zychlinsky Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps J. Cell Biol. 191 2010 677 691
    • (2010) J. Cell Biol. , vol.191 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 31
    • 84866692169 scopus 로고    scopus 로고
    • Perspectives and potential roles for the newly discovered NSP4 in the immune system
    • N.C. Perera, and D.E. Jenne Perspectives and potential roles for the newly discovered NSP4 in the immune system Expert Rev. Clin. Immunol. 8 2012 501 503
    • (2012) Expert Rev. Clin. Immunol. , vol.8 , pp. 501-503
    • Perera, N.C.1    Jenne, D.E.2
  • 33
    • 84883325868 scopus 로고    scopus 로고
    • NSP4 is stored in azurophil granules and released by activated neutrophils as active endoprotease with restricted specificity
    • N.C. Perera, K.-H. Wiesmüller, M.T. Larsen, B. Schacher, P. Eickholz, N. Borregaard, and D.E. Jenne NSP4 is stored in azurophil granules and released by activated neutrophils as active endoprotease with restricted specificity J. Immunol. 191 2013 2700 2707
    • (2013) J. Immunol. , vol.191 , pp. 2700-2707
    • Perera, N.C.1    Wiesmüller, K.-H.2    Larsen, M.T.3    Schacher, B.4    Eickholz, P.5    Borregaard, N.6    Jenne, D.E.7
  • 35
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • C.T.N. Pham Neutrophil serine proteases: specific regulators of inflammation Nat. Rev. Immunol. 6 2006 541 550
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 541-550
    • Pham, C.T.N.1
  • 36
    • 0036892507 scopus 로고    scopus 로고
    • Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways
    • G.A. Preston, C.S. Zarella, W.F. Pendergraft 3rd, E.H. Rudolph, J.J. Yang, S.B. Sekura, J.C. Jennette, and R.J. Falk Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-kappaB and proapoptotic changes in JNK, ERK, and p38 MAPK signaling pathways J. Am. Soc. Nephrol. 13 2002 2840 2849
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2840-2849
    • Preston, G.A.1    Zarella, C.S.2    Pendergraft III, W.F.3    Rudolph, E.H.4    Yang, J.J.5    Sekura, S.B.6    Jennette, J.C.7    Falk, R.J.8
  • 37
    • 51049113366 scopus 로고    scopus 로고
    • Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
    • P. Proost, T. Loos, A. Mortier, E. Schutyser, M. Gouwy, S. Noppen, C. Dillen, I. Ronsse, R. Conings, and S. Struyf et al. Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation J. Exp. Med. 205 2008 2085 2097
    • (2008) J. Exp. Med. , vol.205 , pp. 2085-2097
    • Proost, P.1    Loos, T.2    Mortier, A.3    Schutyser, E.4    Gouwy, M.5    Noppen, S.6    Dillen, C.7    Ronsse, I.8    Conings, R.9    Struyf, S.10
  • 41
    • 73949112004 scopus 로고    scopus 로고
    • ADP-ribosylation of human defensin HNP-1 results in the replacement of the modified arginine with the noncoded amino acid ornithine
    • L.A. Stevens, R.L. Levine, B.R. Gochuico, and J. Moss ADP-ribosylation of human defensin HNP-1 results in the replacement of the modified arginine with the noncoded amino acid ornithine Proc. Natl. Acad. Sci. USA 106 2009 19796 19800
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19796-19800
    • Stevens, L.A.1    Levine, R.L.2    Gochuico, B.R.3    Moss, J.4
  • 42
    • 59849091593 scopus 로고    scopus 로고
    • Citrullination of CXCL12 differentially reduces CXCR4 and CXCR7 binding with loss of inflammatory and anti-HIV-1 activity via CXCR4
    • S. Struyf, S. Noppen, T. Loos, A. Mortier, M. Gouwy, H. Verbeke, D. Huskens, S. Luangsay, M. Parmentier, and K. Geboes et al. Citrullination of CXCL12 differentially reduces CXCR4 and CXCR7 binding with loss of inflammatory and anti-HIV-1 activity via CXCR4 J. Immunol. 182 2009 666 674
    • (2009) J. Immunol. , vol.182 , pp. 666-674
    • Struyf, S.1    Noppen, S.2    Loos, T.3    Mortier, A.4    Gouwy, M.5    Verbeke, H.6    Huskens, D.7    Luangsay, S.8    Parmentier, M.9    Geboes, K.10
  • 46
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: Genes, features and involvement in disease
    • E.R. Vossenaar, A.J.W. Zendman, W.J. van Venrooij, and G.J.M. Pruijn PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease BioEssays 25 2003 1106 1118
    • (2003) BioEssays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.W.2    Van Venrooij, W.J.3    Pruijn, G.J.M.4
  • 47
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • K. Wakasugi, and P. Schimmel Two distinct cytokines released from a human aminoacyl-tRNA synthetase Science 284 1999 147 151
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 48
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • Y. Weinrauch, D. Drujan, S.D. Shapiro, J. Weiss, and A. Zychlinsky Neutrophil elastase targets virulence factors of enterobacteria Nature 417 2002 91 94
    • (2002) Nature , vol.417 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 49
    • 0034614640 scopus 로고    scopus 로고
    • Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding
    • Y. Xu, A. Circolo, H. Jing, Y. Wang, S.V. Narayana, and J.E. Volanakis Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding J. Biol. Chem. 275 2000 378 385
    • (2000) J. Biol. Chem. , vol.275 , pp. 378-385
    • Xu, Y.1    Circolo, A.2    Jing, H.3    Wang, Y.4    Narayana, S.V.5    Volanakis, J.E.6


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