메뉴 건너뛰기




Volumn 348, Issue 5, 2005, Pages 1191-1198

Trypsin inhibition by a peptide hormone: Crystal structure of trypsin-vasopressin complex

Author keywords

Anti diuretic hormone (ADH); Nonapeptide; Trypsin inhibition by a hormone; Trypsin inhibitor; Vasopressin

Indexed keywords

CYSTEINE; DISULFIDE; NEUROPHYSIN; PEPTIDE HORMONE; TRYPSIN; VASOPRESSIN;

EID: 18044391303     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.034     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme-substrate complexes?
    • M. Laskowski Jr, and M.A. Qasim What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme-substrate complexes? Biochim. Biophys. Acta 1477 2000 324 337
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 324-337
    • Laskowski Jr., M.1    Qasim, M.A.2
  • 2
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interactions with proteinases
    • W. Bode, and R. Huber Natural protein proteinase inhibitors and their interactions with proteinases Eur. J. Biochem. 204 1992 433 451
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 3
    • 0017378998 scopus 로고
    • Studies on the synthesis of proteinase inhibitors
    • N. Nishino, H. Aoyagi, T. Kato, and N. Izumiya Studies on the synthesis of proteinase inhibitors J. Biochem. 82 1977 901 909
    • (1977) J. Biochem. , vol.82 , pp. 901-909
    • Nishino, N.1    Aoyagi, H.2    Kato, T.3    Izumiya, N.4
  • 6
    • 0029034507 scopus 로고
    • Synthesis of a mixture of cyclic- peptides based on the Bowman-Birk reactive-site loop to screen for serine-protease inhibitors
    • G.J. Domingo, R.J. Leatherbarrow, N. Freeman, S. Patel, and M. Weir Synthesis of a mixture of cyclic- peptides based on the Bowman-Birk reactive-site loop to screen for serine-protease inhibitors Int. J. Pept. Protein Res. 46 1995 79 87
    • (1995) Int. J. Pept. Protein Res. , vol.46 , pp. 79-87
    • Domingo, G.J.1    Leatherbarrow, R.J.2    Freeman, N.3    Patel, S.4    Weir, M.5
  • 7
    • 0027953720 scopus 로고
    • Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: Chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin
    • Y. Li, Q. Huang, S. Zhang, S. Liu, C. Chi, and Y. Tang Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin J. Biochem. 116 1994 18 25
    • (1994) J. Biochem. , vol.116 , pp. 18-25
    • Li, Y.1    Huang, Q.2    Zhang, S.3    Liu, S.4    Chi, C.5    Tang, Y.6
  • 8
    • 0030795530 scopus 로고    scopus 로고
    • Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases
    • T. Gariani, and R.J. Leatherbarrow Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases J. Pept. Res. 49 1997 467 475
    • (1997) J. Pept. Res. , vol.49 , pp. 467-475
    • Gariani, T.1    Leatherbarrow, R.J.2
  • 9
    • 0029985841 scopus 로고    scopus 로고
    • Comparison of the structures of the cyclotheonamide a complexes of human α-thrombin and bovine β-trypsin
    • V. Ganesh, A.Y. Lee, J. Clardy, and A. Tulinsky Comparison of the structures of the cyclotheonamide A complexes of human α-thrombin and bovine β-trypsin Protein Sci. 5 1996 825 835
    • (1996) Protein Sci. , vol.5 , pp. 825-835
    • Ganesh, V.1    Lee, A.Y.2    Clardy, J.3    Tulinsky, A.4
  • 10
    • 0026050860 scopus 로고
    • Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala chloromethyl ketone an X-ray study at 2.2 Å resolution
    • W.M. Wolf, J. Bajorath, A. Müller, S. Raghunathan, T.P. Singh, W. Hinrichs, and W. Saenger Inhibition of proteinase K by methoxysuccinyl-Ala-Ala- Pro-Ala chloromethyl ketone an X-ray study at 2.2 Å resolution J. Biol. Chem. 266 1991 17695 17699
    • (1991) J. Biol. Chem. , vol.266 , pp. 17695-17699
    • Wolf, W.M.1    Bajorath, J.2    Müller, A.3    Raghunathan, S.4    Singh, T.P.5    Hinrichs, W.6    Saenger, W.7
  • 11
  • 13
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex
    • Q. Huang, S. Liu, and Y. Tang Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex J. Mol. Biol. 229 1993 1022 1036
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 14
    • 0033036045 scopus 로고    scopus 로고
    • Crystal structure of mung bean inhibitor lysine active fragment complex with bovine β-trypsin at 1.8 Å resolution
    • Y. Zhu, Q. Huang, and C. Chi Crystal structure of mung bean inhibitor lysine active fragment complex with bovine β-trypsin at 1.8 Å resolution J. Biomol. Struct. Dynam. 16 1999 1219
    • (1999) J. Biomol. Struct. Dynam. , vol.16 , pp. 1219
    • Zhu, Y.1    Huang, Q.2    Chi, C.3
  • 15
    • 0347481320 scopus 로고    scopus 로고
    • Crystal structure of trypsin-turkey egg white inhibitor complex
    • B. Syed Ibrahim, and V. Pattabhi Crystal structure of trypsin-turkey egg white inhibitor complex Biochem. Biophys. Res. Commun. 313 2003 8 16
    • (2003) Biochem. Biophys. Res. Commun. , vol.313 , pp. 8-16
    • Syed Ibrahim, B.1    Pattabhi, V.2
  • 16
  • 17
    • 18044368197 scopus 로고    scopus 로고
    • Secondary binding site of trypsin: Revealed by crystal structure of trypsin-peptide complex
    • N. Shamaladevi, and V. Pattabhi Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex J. Biomol. Struct. Dynam 2005 In the press
    • (2005) J. Biomol. Struct. Dynam
    • Shamaladevi, N.1    Pattabhi, V.2
  • 18
    • 0014211618 scopus 로고
    • On the size of the active site proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site proteases. I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 19
    • 0003950237 scopus 로고    scopus 로고
    • The pituitary hormones and their control by the hypothalamus
    • 9th edit. Harcourt Brace & Co. Singapore
    • A.C. Guyton, and J.E. Hall The pituitary hormones and their control by the hypothalamus Text Book of Medical Physiology 9th edit. 1998 Harcourt Brace & Co. Singapore 933 944
    • (1998) Text Book of Medical Physiology , pp. 933-944
    • Guyton, A.C.1    Hall, J.E.2
  • 20
    • 0035761657 scopus 로고    scopus 로고
    • Specificity pocket water network and its role in the activity of proteolytic enzymes: Revealed by crystal structures of trypsin
    • A. Johnson, L. Damodharan, and V. Pattabhi Specificity pocket water network and its role in the activity of proteolytic enzymes: revealed by crystal structures of trypsin J. Biochem. Mol. Biol. Biophys. 5 2001 559 565
    • (2001) J. Biochem. Mol. Biol. Biophys. , vol.5 , pp. 559-565
    • Johnson, A.1    Damodharan, L.2    Pattabhi, V.3
  • 22
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrate of trypsin
    • B.F. Erlanger, N. Kokowsky, and W. Cohen The preparation and properties of two new chromogenic substrate of trypsin Arch. Biochem. Biophys. 95 1961 271 278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 23
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
    • N.A. Ranson, S.G. Burston, and A.R. Clarke Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction J. Mol. Biol. 266 1997 656 664
    • (1997) J. Mol. Biol. , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 24
    • 0004024383 scopus 로고
    • 2nd edit. VCH Publication Verlagesgesellschaft, Weinheim
    • H. Zollner Handbook of Enzyme Inhibitors 2nd edit. 1993 VCH Publication Verlagesgesellschaft, Weinheim
    • (1993) Handbook of Enzyme Inhibitors
    • Zollner, H.1
  • 27
    • 0032724963 scopus 로고    scopus 로고
    • Crystal structure at 1.63 Å resolution of the native form of porcine β-trypsin: Revealing an acetate ion binding site and functional water network
    • A. Johnson, N. Gautham, and V. Pattabhi Crystal structure at 1.63 Å resolution of the native form of porcine β-trypsin: revealing an acetate ion binding site and functional water network Biochim. Biophys. Acta 1435 1999 7 21
    • (1999) Biochim. Biophys. Acta , vol.1435 , pp. 7-21
    • Johnson, A.1    Gautham, N.2    Pattabhi, V.3
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
  • 31
    • 0034842483 scopus 로고    scopus 로고
    • Structures of an unliganded neurophysin and its vasopressin complex: Implications for binding and allosteric mechanisms
    • C.K. Wu, B. Hu, J.P. Rose, Z.J. Liu, T.L. Nguyen, and C. Zeng Structures of an unliganded neurophysin and its vasopressin complex: implications for binding and allosteric mechanisms Protein Sci. 10 2001 1869 1880
    • (2001) Protein Sci. , vol.10 , pp. 1869-1880
    • Wu, C.K.1    Hu, B.2    Rose, J.P.3    Liu, Z.J.4    Nguyen, T.L.5    Zeng, C.6
  • 32
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution
    • R. Voss, U. Ermler, L. Essen, G. Wenzl, Y. Kim, and P. Flecker Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution Eur. J. Biochem. 242 1996 122 131
    • (1996) Eur. J. Biochem. , vol.242 , pp. 122-131
    • Voss, R.1    Ermler, U.2    Essen, L.3    Wenzl, G.4    Kim, Y.5    Flecker, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.