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Volumn 279, Issue 24, 2012, Pages 4466-4478

Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin

Author keywords

disulfide bond; Kazal; protease inhibitor complex; specificity; thermostability

Indexed keywords

ACETONITRILE; APROTININ; CHYMOTRYPSIN; DISULFIDE; GREGLIN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 84870503884     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12033     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 42249109450 scopus 로고    scopus 로고
    • Serine peptidases: Classification, structure and function
    • Page MJ, &, Di Cera E, (2008) Serine peptidases: classification, structure and function. Cell Mol Life Sci 65, 1220-1236.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1220-1236
    • Page, M.J.1    Di Cera, E.2
  • 3
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings ND, Barrett AJ, &, Bateman A, (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 40, D343-D350.
    • (2012) Nucleic Acids Res , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 4
    • 0015785093 scopus 로고
    • Trypsin-pancreatic secretory inhibitor (Kazal inhibitor) interaction. Kinetic and thermodynamic properties
    • Schweitz H, Vincent JP, &, Lazdunski M, (1973) Trypsin-pancreatic secretory inhibitor (Kazal inhibitor) interaction. Kinetic and thermodynamic properties. Biochemistry 12, 2841-2846.
    • (1973) Biochemistry , vol.12 , pp. 2841-2846
    • Schweitz, H.1    Vincent, J.P.2    Lazdunski, M.3
  • 5
    • 0022034438 scopus 로고
    • The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)
    • Bode W, Epp O, Huber R, Laskowski M Jr, &, Ardelt W, (1985) The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). Eur J Biochem 147, 387-395.
    • (1985) Eur J Biochem , vol.147 , pp. 387-395
    • Bode, W.1    Epp, O.2    Huber, R.3    Laskowski Jr., M.4    Ardelt, W.5
  • 6
    • 0023198896 scopus 로고
    • Crystal and molecular structures of the complex of α-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution
    • Fujinaga M, Sielecki AR, Read RJ, Ardelt W, Laskowski M Jr, &, James MN, (1987) Crystal and molecular structures of the complex of α-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution. J Mol Biol 195, 397-418.
    • (1987) J Mol Biol , vol.195 , pp. 397-418
    • Fujinaga, M.1    Sielecki, A.R.2    Read, R.J.3    Ardelt, W.4    Laskowski Jr., M.5    James, M.N.6
  • 7
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, &, Berger A, (1967) On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27, 157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 9
    • 22244438235 scopus 로고    scopus 로고
    • Structural and functional study of an Anemonia elastase inhibitor, a 'nonclassical' Kazal-type inhibitor from Anemonia sulcata
    • Hemmi H, Kumazaki T, Yoshizawa-Kumagaye K, Nishiuchi Y, Yoshida T, Ohkubo T, &, Kobayashi Y, (2005) Structural and functional study of an Anemonia elastase inhibitor, a 'nonclassical' Kazal-type inhibitor from Anemonia sulcata. Biochemistry 44, 9626-9636.
    • (2005) Biochemistry , vol.44 , pp. 9626-9636
    • Hemmi, H.1    Kumazaki, T.2    Yoshizawa-Kumagaye, K.3    Nishiuchi, Y.4    Yoshida, T.5    Ohkubo, T.6    Kobayashi, Y.7
  • 15
    • 0041347814 scopus 로고    scopus 로고
    • Structure and energetics of protein-protein interactions: The role of conformational heterogeneity in OMTKY3 binding to serine proteases
    • Horn JR, Ramaswamy S, &, Murphy KP, (2003) Structure and energetics of protein-protein interactions: the role of conformational heterogeneity in OMTKY3 binding to serine proteases. J Mol Biol 331, 497-508.
    • (2003) J Mol Biol , vol.331 , pp. 497-508
    • Horn, J.R.1    Ramaswamy, S.2    Murphy, K.P.3
  • 16
    • 79955575381 scopus 로고    scopus 로고
    • Structural basis for dual-inhibition mechanism of a non-classical Kazal-type serine protease inhibitor from horseshoe crab in complex with subtilisin
    • Shenoy RT, Thangamani S, Velazquez-Campoy A, Ho B, Ding JL, &, Sivaraman J, (2011) Structural basis for dual-inhibition mechanism of a non-classical Kazal-type serine protease inhibitor from horseshoe crab in complex with subtilisin. PLoS One 6, e18838.
    • (2011) PLoS One , vol.6
    • Shenoy, R.T.1    Thangamani, S.2    Velazquez-Campoy, A.3    Ho, B.4    Ding, J.L.5    Sivaraman, J.6
  • 17
    • 0029833222 scopus 로고    scopus 로고
    • The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies
    • Fujinaga M, Chernaia MM, Halenbeck R, Koths K, &, James MN, (1996) The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies. J Mol Biol 261, 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
  • 18
    • 0025978283 scopus 로고
    • α trace application to model building and detection of co-ordinate errors
    • α trace application to model building and detection of co-ordinate errors. J Mol Biol 218, 183-194.
    • (1991) J Mol Biol , vol.218 , pp. 183-194
    • Holm, L.1    Sander, C.2
  • 20
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht A, Lamba D, Bauer M, Huber R, Friedrich T, Kroger B, Hoffken W, &, Bode W, (1995) Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 14, 5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • Van De Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kroger, B.6    Hoffken, W.7    Bode, W.8
  • 21
    • 0025737887 scopus 로고
    • Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type)
    • Hecht HJ, Szardenings M, Collins J, &, Schomburg D, (1991) Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). J Mol Biol 220, 711-722.
    • (1991) J Mol Biol , vol.220 , pp. 711-722
    • Hecht, H.J.1    Szardenings, M.2    Collins, J.3    Schomburg, D.4
  • 25
    • 0028242139 scopus 로고
    • Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy
    • Liepinsh E, Berndt KD, Sillard R, Mutt V, &, Otting G, (1994) Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy. J Mol Biol 239, 137-153.
    • (1994) J Mol Biol , vol.239 , pp. 137-153
    • Liepinsh, E.1    Berndt, K.D.2    Sillard, R.3    Mutt, V.4    Otting, G.5
  • 26
    • 77956896622 scopus 로고    scopus 로고
    • Isolation, cDNA cloning, and structure-based functional characterization of oryctin, a hemolymph protein from the coconut rhinoceros beetle, Oryctes rhinoceros, as a novel serine protease inhibitor
    • Horita S, Ishibashi J, Nagata K, Miyakawa T, Yamakawa M, &, Tanokura M, (2010) Isolation, cDNA cloning, and structure-based functional characterization of oryctin, a hemolymph protein from the coconut rhinoceros beetle, Oryctes rhinoceros, as a novel serine protease inhibitor. J Biol Chem 285, 30150-30158.
    • (2010) J Biol Chem , vol.285 , pp. 30150-30158
    • Horita, S.1    Ishibashi, J.2    Nagata, K.3    Miyakawa, T.4    Yamakawa, M.5    Tanokura, M.6
  • 27
    • 0027489832 scopus 로고
    • Thermodynamics of unfolding for turkey ovomucoid third domain: Thermal and chemical denaturation
    • Swint L, &, Robertson AD, (1993) Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci 2, 2037-2049.
    • (1993) Protein Sci , vol.2 , pp. 2037-2049
    • Swint, L.1    Robertson, A.D.2
  • 28
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell S, &, Argos P, (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol 269, 631-643.
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 29
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulphide bonds
    • Matsumura M, Signor G, &, Matthews BW, (1989) Substantial increase of protein stability by multiple disulphide bonds. Nature 342, 291-293.
    • (1989) Nature , vol.342 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Matthews, B.W.3
  • 30
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • Thompson MJ, &, Eisenberg D, (1999) Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability. J Mol Biol 290, 595-604.
    • (1999) J Mol Biol , vol.290 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 31
    • 0027412820 scopus 로고
    • Binding of amino acid side chains to preformed cavities: Interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues
    • Bigler TL, Lu W, Park SJ, Tashiro M, Wieczorek M, Wynn R, &, Laskowski M Jr, (1993) Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues. Protein Sci 2, 786-799.
    • (1993) Protein Sci , vol.2 , pp. 786-799
    • Bigler, T.L.1    Lu, W.2    Park, S.J.3    Tashiro, M.4    Wieczorek, M.5    Wynn, R.6    Laskowski Jr., M.7
  • 32
    • 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, &, Kellenberger C, (2001) Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity. J Biol Chem 276, 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
  • 33
    • 0344823663 scopus 로고    scopus 로고
    • Selective inhibition of trypsins by insect peptides: Role of P6-P10 loop
    • Kellenberger C, Ferrat G, Leone P, Darbon H, &, Roussel A, (2003) Selective inhibition of trypsins by insect peptides: role of P6-P10 loop. Biochemistry 42, 13605-13612.
    • (2003) Biochemistry , vol.42 , pp. 13605-13612
    • Kellenberger, C.1    Ferrat, G.2    Leone, P.3    Darbon, H.4    Roussel, A.5
  • 34
    • 79953304264 scopus 로고    scopus 로고
    • Structure-function analysis of grass clip serine protease involved in Drosophila Toll pathway activation
    • Kellenberger C, Leone P, Coquet L, Jouenne T, Reichhart JM, &, Roussel A, (2011) Structure-function analysis of grass clip serine protease involved in Drosophila Toll pathway activation. J Biol Chem 286, 12300-12307.
    • (2011) J Biol Chem , vol.286 , pp. 12300-12307
    • Kellenberger, C.1    Leone, P.2    Coquet, L.3    Jouenne, T.4    Reichhart, J.M.5    Roussel, A.6
  • 35
    • 20444474984 scopus 로고    scopus 로고
    • Deletion of the 60-loop provides new insights into the substrate and inhibitor specificity of thrombin
    • Rezaie AR, &, Yang L, (2005) Deletion of the 60-loop provides new insights into the substrate and inhibitor specificity of thrombin. Thromb Haemost 93, 1047-1054.
    • (2005) Thromb Haemost , vol.93 , pp. 1047-1054
    • Rezaie, A.R.1    Yang, L.2
  • 36
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of d -Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W, Turk D, &, Karshikov A, (1992) The refined 1.9-Å X-ray crystal structure of d -Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1, 426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 37
    • 34547733426 scopus 로고    scopus 로고
    • The role of autolysis loop in determining the specificity of coagulation proteases
    • Yang L, Manithody C, &, Rezaie AR, (2007) The role of autolysis loop in determining the specificity of coagulation proteases. Braz J Med Biol Res 40, 1055-1064.
    • (2007) Braz J Med Biol Res , vol.40 , pp. 1055-1064
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 38
    • 44949182000 scopus 로고    scopus 로고
    • Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
    • Korkmaz B, Attucci S, Juliano MA, Kalupov T, Jourdan ML, Juliano L, &, Gauthier F, (2008) Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates. Nat Protoc 3, 991-1000.
    • (2008) Nat Protoc , vol.3 , pp. 991-1000
    • Korkmaz, B.1    Attucci, S.2    Juliano, M.A.3    Kalupov, T.4    Jourdan, M.L.5    Juliano, L.6    Gauthier, F.7
  • 40
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P, (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62, 72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 41
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza J, (2001) Implementation of molecular replacement in AMoRe. Acta Crystallogr D Biol Crystallogr 57, 1367-1372.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1367-1372
    • Navaza, J.1


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