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Volumn 258, Issue 1, 1996, Pages 158-171

Solution structure of PMP-C: A new fold in the group of small serine proteinase inhibitors

Author keywords

Calcium channel blocker; Disulfide bridge; Locusta migratoria; NMR; Proteinase inhibitor

Indexed keywords

CALCIUM CHANNEL BLOCKING AGENT; PHENYL GROUP; SERINE PROTEINASE INHIBITOR;

EID: 0030004582     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0240     Document Type: Article
Times cited : (51)

References (45)
  • 1
    • 46549098930 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985). MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 61, 306-320.
    • (1985) J. Magn. Reson. , vol.61 , pp. 306-320
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W. & Huber, R. (1992). Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 3
    • 0023643147 scopus 로고
    • The high resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode, W., Papamokos, E. & Musil, D. (1987). The high resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur. J. Biochem. 166, 673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 4
    • 0024959382 scopus 로고
    • The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima)
    • Bode, W., Greyling, H. J., Huber, R., Otlewski, J. & Wilusz, T. (1989). The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). FEBS Letters, 242, 285-292.
    • (1989) FEBS Letters , vol.242 , pp. 285-292
    • Bode, W.1    Greyling, H.J.2    Huber, R.3    Otlewski, J.4    Wilusz, T.5
  • 5
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. & Ruben, D. J. (1980). Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters, 69, 185-189.
    • (1980) Chem. Phys. Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 7
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems, F., Roumestand, C., Gilquin, B., Ménez, A. & Toma, F. (1991). Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science, 254, 1521-1523.
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Ménez, A.4    Toma, F.5
  • 8
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R. R. (1983). Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 9
    • 0017848335 scopus 로고
    • The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor
    • Brown, L. R., De Marco, A., Richarz, R., Wagner, G. & Wüthrich, K. (1978). The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor. Eur. J. Biochem. 88, 87-95.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 87-95
    • Brown, L.R.1    De Marco, A.2    Richarz, R.3    Wagner, G.4    Wüthrich, K.5
  • 11
    • 49349130990 scopus 로고
    • Spin-spin coupling and the conformational states of peptide systems
    • Bystrov, V. F. (1976). Spin-spin coupling and the conformational states of peptide systems. Prog. Nucl. Magn. Reson. Spectrosc. 10, 41-82.
    • (1976) Prog. Nucl. Magn. Reson. Spectrosc. , vol.10 , pp. 41-82
    • Bystrov, V.F.1
  • 12
    • 0024351231 scopus 로고
    • Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy
    • Clore, G. M. & Gronenborn, A. M. (1989). Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy Crit. Rev. Biochem. Mol. Biol. 24, 479-564.
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 479-564
    • Clore, G.M.1    Gronenborn, A.M.2
  • 13
    • 0028773904 scopus 로고
    • High-resolution structure of Ascaris trypsin inhibitor in solution: Direct evidence for a pH-induced conformational transition in the reactive site
    • Grasberger, B. L., Clore, G. M. & Gronenborn, A. M. (1994). High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure, 2, 669-678.
    • (1994) Structure , vol.2 , pp. 669-678
    • Grasberger, B.L.1    Clore, G.M.2    Gronenborn, A.M.3
  • 15
    • 30244576420 scopus 로고
    • Solid-phase synthesis of a 36 amino acid fucopeptide with the uncommon Thr-Fuc linkage
    • Hietter, H., Schultz, M. & Kunz, H. (1995). Solid-phase synthesis of a 36 amino acid fucopeptide with the uncommon Thr-Fuc linkage. Syn. Letter, 12, 1219.
    • (1995) Syn. Letter , vol.12 , pp. 1219
    • Hietter, H.1    Schultz, M.2    Kunz, H.3
  • 16
    • 0024828095 scopus 로고
    • Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop
    • Holak, T. A., Bode, W., Huber, R., Otlewski, J. & Wilusz, T. (1989a). Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop. J. Mol. Biol. 210, 649-654.
    • (1989) J. Mol. Biol. , vol.210 , pp. 649-654
    • Holak, T.A.1    Bode, W.2    Huber, R.3    Otlewski, J.4    Wilusz, T.5
  • 17
    • 0024815191 scopus 로고
    • Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing
    • Holak, T. A., Gondol, D., Otlewski, J. & Wilusz, T. (1989b). Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing. J. Mol. Biol. 210, 635-648.
    • (1989) J. Mol. Biol. , vol.210 , pp. 635-648
    • Holak, T.A.1    Gondol, D.2    Otlewski, J.3    Wilusz, T.4
  • 18
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang, K., Strynadka, N. C. J., Bernard, V. D., Peanasky, R. J. & James, M. N. G. (1994). The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure, 2, 679-689.
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.J.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.G.5
  • 19
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles
    • Hyberts, S. G., Märki, W. & Wagner, G. (1987). Stereospecific assignments of side-chain protons and characterization of torsion angles. Eur. J. Biochem. 164, 625-635.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Märki, W.2    Wagner, G.3
  • 20
    • 0027438789 scopus 로고
    • Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its glycoforms
    • Joao, H. C. & Dwek, R. A. (1993). Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its glycoforms. Eur. J. Biochem. 218, 239-244.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 239-244
    • Joao, H.C.1    Dwek, R.A.2
  • 21
    • 33745356391 scopus 로고
    • Contact electron-spin interactions of nuclear magnetic moments
    • Karplus, M. (1959). Contact electron-spin interactions of nuclear magnetic moments. J. Chem. Phys. 30, 11-15.
    • (1959) J. Chem. Phys. , vol.30 , pp. 11-15
    • Karplus, M.1
  • 22
    • 0028826920 scopus 로고
    • Serine protease inhibition by insect peptides containing a cystine-knot and a triple-stranded β-sheet
    • Kellenberger, C., Boudier, C., Bermudez, I., Bieth, J. G., Luu, B. & Hietter, H. (1995). Serine protease inhibition by insect peptides containing a cystine-knot and a triple-stranded β-sheet. J. Biol. Chem. 270, 25514-25519.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25514-25519
    • Kellenberger, C.1    Boudier, C.2    Bermudez, I.3    Bieth, J.G.4    Luu, B.5    Hietter, H.6
  • 23
    • 0027236599 scopus 로고
    • Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data
    • Klaus, W., Broger, C., Gerber, P. & Senn, H. (1993). Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. J. Mol. Biol. 232, 897-906.
    • (1993) J. Mol. Biol. , vol.232 , pp. 897-906
    • Klaus, W.1    Broger, C.2    Gerber, P.3    Senn, H.4
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 25
    • 0028388768 scopus 로고
    • Cloning of a Locusta cDNA encoding a precursor peptide for two structurally related proteinase inhibitors
    • Kromer, E., Nakakura, N. & Lagueux, M. (1994). Cloning of a Locusta cDNA encoding a precursor peptide for two structurally related proteinase inhibitors. Insect Biochem. Mol. Biol. 24, 329-331.
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 329-331
    • Kromer, E.1    Nakakura, N.2    Lagueux, M.3
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0000660695 scopus 로고    scopus 로고
    • Structural dynamics of PMP-D2: An experimental and theoretical study
    • Mer, G., Dejaegere, A., Stote, R., Kieffer, B. & Lefèvre, J.-F. (1996). Structural dynamics of PMP-D2: an experimental and theoretical study. J. Phys. Chem. 100, 2667-2674.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2667-2674
    • Mer, G.1    Dejaegere, A.2    Stote, R.3    Kieffer, B.4    Lefèvre, J.-F.5
  • 30
    • 0001503921 scopus 로고
    • Chain-folding initiation structures in ribonuclease A: Conformational analysis of trans-Ac-Asn-Pro-Tyr-NHMe and trans-Ac-Tyr-Pro-Asn-NHMe in water and in the solid state
    • Montelione, G. T., Arnold, E., Meinwald, Y. C., Stimson, E. R., Denton, J. B., Huang, S.-G., Clardy J. & Scheraga, H. A. (1984). Chain-folding initiation structures in ribonuclease A: conformational analysis of trans-Ac-Asn-Pro-Tyr-NHMe and trans-Ac-Tyr-Pro-Asn-NHMe in water and in the solid state. J. Am. Chem. Soc. 106, 7946-7958.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7946-7958
    • Montelione, G.T.1    Arnold, E.2    Meinwald, Y.C.3    Stimson, E.R.4    Denton, J.B.5    Huang, S.-G.6    Clardy, J.7    Scheraga, H.A.8
  • 31
    • 0026567538 scopus 로고
    • Isolation and structural determination of three peptides from the insect Locusta migratoria
    • Nakakura, N., Hietter, H., van Dorsselaer, A. & Luu, B. (1992). Isolation and structural determination of three peptides from the insect Locusta migratoria. Eur. J. Biochem. 204, 147-153.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 147-153
    • Nakakura, N.1    Hietter, H.2    Van Dorsselaer, A.3    Luu, B.4
  • 32
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy P. K., Nielsen, K. J., Craik, D. J. & Norton, R. S. (1994). A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3, 1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 33
  • 34
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR, 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 35
    • 0015874675 scopus 로고
    • Conformational studies on a glycosylated bovine pancreatic ribonuclease
    • Puett, D. (1973). Conformational studies on a glycosylated bovine pancreatic ribonuclease. J. Biol. Chem. 248, 3566-3572.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3566-3572
    • Puett, D.1
  • 37
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. (1981). The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34, 167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.1
  • 38
    • 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
  • 39
    • 0021317946 scopus 로고
    • On the genetic and structural similarities between the squash seeds polypeptide trypsin inhibitors and wheat germ agglutinin
    • Siemion, I. Z., Wilusz, T. & Polanowski, A. (1984). On the genetic and structural similarities between the squash seeds polypeptide trypsin inhibitors and wheat germ agglutinin. Mol. Cell. Biochem. 60, 159-161.
    • (1984) Mol. Cell. Biochem. , vol.60 , pp. 159-161
    • Siemion, I.Z.1    Wilusz, T.2    Polanowski, A.3
  • 41
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton, J. M. (1981). Disulphide bridges in globular proteins. J. Mol. Biol. 151, 261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 42
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, W., Havel, T. F., Schaumann, T., Go, N. & Wüthrich, K. (1987). Protein structures in solution by nuclear magnetic resonance and distance geometry The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196, 611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 44
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1992). The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry, 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


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