메뉴 건너뛰기




Volumn 42, Issue 46, 2003, Pages 13605-13612

Selective Inhibition of Trypsins by Insect Peptides: Role of P6-P10 Loop

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CRYSTAL STRUCTURE; FUNGI; NUCLEAR MAGNETIC RESONANCE;

EID: 0344823663     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035318t     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain, Biochem. Biophys. Res. Commun. 27, 157-62.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 2
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzymes substrate complexes?
    • Laskowski, M. J., and Qasim, M. A. (2000) What can the structures of enzyme-inhibitor complexes tell us about the structures of enzymes substrate complexes? Biochim. Biophys. Acta 1477, 324-337.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 324-337
    • Laskowski, M.J.1    Qasim, M.A.2
  • 4
    • 0028826920 scopus 로고
    • Serine protease inhibition by insect peptide containing a cysteine-knot and a triple-stranded β-sheet
    • Kellenberger, C., Boudier, C., Bermudez, I., Bieth, J. G., Luu, B., and Hietter, H. (1995) Serine protease inhibition by insect peptide containing a cysteine-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
  • 5
    • 0032709689 scopus 로고    scopus 로고
    • Proteinase inhibitors from desert locust Schistocerca gregaria: Engineering both P1 and P1′ residues converts a potent chymotrypsin inhibitor to a potent trypsin inhibitor
    • Malik, Z., Amir, S., Pál, G., Buzás, Z., Várallyay, E., Antal, J., Szilágyi, Z., Vékey, K., Asbóth, B., Patthy, A., and Gráf, L. (1999) Proteinase inhibitors from desert locust Schistocerca gregaria: engineering both P1 and P1′ residues converts a potent chymotrypsin inhibitor to a potent trypsin inhibitor, Biochim. Biophys. Acta 1434, 143-150.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 143-150
    • Malik, Z.1    Amir, S.2    Pál, G.3    Buzás, Z.4    Várallyay, E.5    Antal, J.6    Szilágyi, Z.7    Vékey, K.8    Asbóth, B.9    Patthy, A.10    Gráf, L.11
  • 7
    • 0030004582 scopus 로고    scopus 로고
    • Solution structure of PMP-C: A new fold in the group of small proteinase inhibitors
    • Mer, G., Kellenberger, C., Renatus, M., Luu, B., Hietter, H., and Lefèvre, J.-F. (1996) Solution structure of PMP-C: a new fold in the group of small proteinase inhibitors, J. Mol. Biol. 258, 158-171.
    • (1996) J. Mol. Biol. , vol.258 , pp. 158-171
    • Mer, G.1    Kellenberger, C.2    Renatus, M.3    Luu, B.4    Hietter, H.5    Lefèvre, J.-F.6
  • 8
    • 0036161755 scopus 로고    scopus 로고
    • Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria
    • Gaspari, Z., Patthy, A., Graf, L., and Perczel, A. (2002) Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria, Eur. J. Biochem. 269, 527-37.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 527-537
    • Gaspari, Z.1    Patthy, A.2    Graf, L.3    Perczel, A.4
  • 9
    • 0035914320 scopus 로고    scopus 로고
    • Complexation of two proteic insect inhibitors to chymotrypsin's active site suggests decoupled roles for binding and selectivity
    • Roussel, A., Mathieu, M., Dobbs, A., Luu, B., Cambillau, C., and Kellenberger, C. (2001) Complexation of two proteic insect inhibitors to chymotrypsin's active site 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
  • 11
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. (1995) Theoretical and practical aspects of proteinase inhibition kinetics, Methods Enzymol. 248, 59-84.
    • (1995) Methods Enzymol. , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 12
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T., Billeter, M., Guntert, P., and Wuthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 5, 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 14
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Guntert, P., and Wuthrich, K. (1991) Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints, J. Biomol. NMR 1, 447-56.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Guntert, P.1    Wuthrich, K.2
  • 15
    • 0035980211 scopus 로고    scopus 로고
    • Solution structure of Ptul, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type
    • Bernard, C., Corzo, G., Mosbah, A., Nakajima, T., and Darbon, H. (2001) Solution structure of Ptul, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type, Biochemistry 40, 12795-800.
    • (2001) Biochemistry , vol.40 , pp. 12795-12800
    • Bernard, C.1    Corzo, G.2    Mosbah, A.3    Nakajima, T.4    Darbon, H.5
  • 17
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-86.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 18
    • 0000660695 scopus 로고    scopus 로고
    • Structural dynamics of PMP-D2: An experimental and theorical study
    • Mer, G., Dejeagere, A., Stote, R., Kieffer, B., and Lefèvre, J. F. (1996) Structural dynamics of PMP-D2: an experimental and theorical study, J. Phys. Chem. 100, 2667-2674.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2667-2674
    • Mer, G.1    Dejeagere, A.2    Stote, R.3    Kieffer, B.4    Lefèvre, J.F.5
  • 19
    • 0033958060 scopus 로고    scopus 로고
    • Characterisation of multiple trypsins from the midgut of Locusta migratoria
    • Lam, W., Coast, G. M., and Rayne, R. C. (2000) Characterisation of multiple trypsins from the midgut of Locusta migratoria, Insect Biochem. Mol. Biol. 30, 85-94.
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 85-94
    • Lam, W.1    Coast, G.M.2    Rayne, R.C.3
  • 20
    • 0033485402 scopus 로고    scopus 로고
    • Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library
    • McBride, J. D., Freeman, H. N., and Leatherbarrow, R. J. (1999) Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library, Eur. J. Biochem. 266, 403-12.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 403-412
    • McBride, J.D.1    Freeman, H.N.2    Leatherbarrow, R.J.3
  • 21
    • 0037672714 scopus 로고    scopus 로고
    • The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2
    • Radisky, E. S., King, D. S., Kwan, G., and Koshland, D. E., Jr. (2003) The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2, Biochemistry 42, 6484-92.
    • (2003) Biochemistry , vol.42 , pp. 6484-6492
    • Radisky, E.S.1    King, D.S.2    Kwan, G.3    Koshland Jr., D.E.4
  • 22
    • 0028266885 scopus 로고
    • Macromomecular chelation as an improved mechanism of protease inhibition: Structure of the ecotin-trypsin complex
    • McGrath, M. E., Erpel, T., Bystroff, C., and Fletterick, R. (1994) Macromomecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex. EMBO J. 13, 1502-1507.
    • (1994) EMBO J. , vol.13 , pp. 1502-1507
    • McGrath, M.E.1    Erpel, T.2    Bystroff, C.3    Fletterick, R.4
  • 23
    • 0028388768 scopus 로고
    • Cloning of a Locusta cDNA encoding a precursor peptide for two structurally related proteinase inhibitors
    • Kromer, E., Nakakura, N., and 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
  • 24
    • 0037085228 scopus 로고    scopus 로고
    • Remarkable phylum selectivity of a Schistocerca gregaria trypsin inhibitor: The possible role of enzyme-inhibitor flexibility
    • Patthy, A., Amir, S., Malik, Z., Bodi, A., Kardos, J., Asboth, B., and Graf, L. (2002) Remarkable phylum selectivity of a Schistocerca gregaria trypsin inhibitor: the possible role of enzyme-inhibitor flexibility, Arch Biochem. Biophys. 398, 179-87.
    • (2002) Arch Biochem. Biophys. , vol.398 , pp. 179-187
    • Patthy, A.1    Amir, S.2    Malik, Z.3    Bodi, A.4    Kardos, J.5    Asboth, B.6    Graf, L.7
  • 25
    • 0015387337 scopus 로고
    • Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges
    • Vincent, J. P., and Lazdunski, M. (1972) Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges, Biochemistry 11, 2967-2977.
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.P.1    Lazdunski, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.