메뉴 건너뛰기




Volumn 7, Issue 4, 2000, Pages 322-328

Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE A; ENZYME INHIBITOR;

EID: 0343569968     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/74092     Document Type: Article
Times cited : (73)

References (43)
  • 1
    • 0032484025 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression and characterization
    • Reverter, D., et al. A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression and characterization. J. Biol. Chem. 273, 32927-32933 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32927-32933
    • Reverter, D.1
  • 2
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W. & Drayna, D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266, 21833-21838 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 3
    • 0024370747 scopus 로고
    • Cloning of cDNAs that encode human mast cell carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase a and rat pancreatic carboxypeptidases
    • Reynolds, D.S., et al. Cloning of cDNAs that encode human mast cell carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases. Proc. Natl Acad. Sci. USA 86, 9480-9484 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9480-9484
    • Reynolds, D.S.1
  • 4
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. a study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, M., Gronenborn, A.M, Nilges, M. & Ryan, C.A. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 26,8012-8023 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 5
    • 0020491126 scopus 로고
    • Refined crystal structure of the potato inhibitor complex of carboxypeptidase a at 2.5 a resolution
    • Rees, D.C. & Lipscomb, W.N. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution. J. Mol. Biol. 160, 475-498 (1982).
    • (1982) J. Mol. Biol. , vol.160 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 6
    • 0027516469 scopus 로고
    • Advances in metalloprocarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process
    • Aviles, FX., Vendrell, J., Guasch, A., Coll, M & Huber R. Advances in metalloprocarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process. Eur J Biochem. 211, 381-389 (1993).
    • (1993) Eur J Biochem. , vol.211 , pp. 381-389
    • Aviles, F.X.1    Vendrell, J.2    Guasch, A.3    Coll, M.4    Huber, R.5
  • 7
    • 0027932407 scopus 로고
    • C-tail valine is a key residue for stabilization of complex between potato inhibitor and carboxypeptidase a
    • Molina, M.A., Marino, C., Oliva, B., Aviles, F.X. & Querol, E. C-tail valine is a key residue for stabilization of complex between potato inhibitor and carboxypeptidase A. J Biol. Chem. 269, 21467-21472 (1994).
    • (1994) J Biol. Chem. , vol.269 , pp. 21467-21472
    • Molina, M.A.1    Marino, C.2    Oliva, B.3    Aviles, F.X.4    Querol, E.5
  • 8
    • 0023189460 scopus 로고
    • Isolation and characterization of antistasin. an inhibitor of metastasis and coagulation
    • Tuszynski, G.P., Gasic, T.B. & Gasic, G.J. Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation. J. Biol. Chem. 262, 9718-9723 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 9718-9723
    • Tuszynski, G.P.1    Gasic, T.B.2    Gasic, G.J.3
  • 9
    • 0025329390 scopus 로고
    • The structure of a complex of recombinant hirudin and human alpha-thrombin
    • Rydel, T.J., et al. The structure of a complex of recombinant hirudin and human alpha-thrombin. Science 249, 277-280 (1990).
    • (1990) Science , vol.249 , pp. 277-280
    • Rydel, T.J.1
  • 10
    • 0022701771 scopus 로고
    • Refined 1.2 a crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin
    • Bode, W., Papamokos, E., Musil, D., Seemuller, U. & Fritz, H. Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin. EMBO J. 5, 813-8 (1986).
    • (1986) EMBO J. , vol.5 , pp. 813-818
    • Bode, W.1    Papamokos, E.2    Musil, D.3    Seemuller, U.4    Fritz, H.5
  • 11
    • 0025475107 scopus 로고
    • X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 a resolution
    • Bolognesi, M., et al. X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution. J Mol. Recognit. 3, 163-168 (1990).
    • (1990) J Mol. Recognit. , vol.3 , pp. 163-168
    • Bolognesi, M.1
  • 12
    • 0031568813 scopus 로고    scopus 로고
    • A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex
    • Mittl, P.R.. et al. A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex. Structure 5, 253-264 (1997).
    • (1997) Structure , vol.5 , pp. 253-264
    • Mittl, P.R.1
  • 13
    • 0027944325 scopus 로고
    • Structure of leech derived tryptase inhibitor (LDTI-C) in solution
    • Mühlhahn, P., et al. Structure of leech derived tryptase inhibitor (LDTI-C) in solution. FEBS Lett. 355, 290-296 (1994).
    • (1994) FEBS Lett. , vol.355 , pp. 290-296
    • Mühlhahn, P.1
  • 14
    • 0030754090 scopus 로고    scopus 로고
    • The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition
    • Stubbs, M.T., et al. The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition. J. Biol. Chem. 272, 19931-19937 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 19931-19937
    • Stubbs, M.T.1
  • 15
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar, L, Manuel, R. & Nesheim, M.E. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 270, 14477-14484 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 16
    • 0030920922 scopus 로고    scopus 로고
    • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
    • Sakharov D.V., Plow, E.F. & Rijken, C. On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. J. Biol. Chem. 272, 14477-14482 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 14477-14482
    • Sakharov, D.V.1    Plow, E.F.2    Rijken, C.3
  • 17
    • 0025139697 scopus 로고
    • Distribution of intestinal mast cell proteinase in blood and tissues of normal and Trichinella-infected mice
    • Huntley, J.F., et al. Distribution of intestinal mast cell proteinase in blood and tissues of normal and Trichinella-infected mice. Parasite Immunol. 12, 85-95 (1990).
    • (1990) Parasite Immunol. , vol.12 , pp. 85-95
    • Huntley, J.F.1
  • 18
    • 0029738315 scopus 로고    scopus 로고
    • Lung granulomatous response induced by infection with the intestinal nematode Nippostrongylus brasiliensis is suppressed in mast cell-deficient Ws/Ws rats
    • Arizono, N., eta/. Lung granulomatous response induced by infection with the intestinal nematode Nippostrongylus brasiliensis is suppressed in mast cell-deficient Ws/Ws rats. Clin. Exp. Immunol. 106, 55-61 (1996).
    • (1996) Clin. Exp. Immunol. , vol.106 , pp. 55-61
    • Arizono, N.1
  • 19
    • 0040974381 scopus 로고    scopus 로고
    • The threedimensional structure of human procarboxypeptidase A2. Deciphering the basis of its inhibition, activation and intrinsic activity of the zymogen
    • Garcia-Sáez, I., Reverter, D., Vendrell, J, Aviles, F.X. & Coll, M. The threedimensional structure of human procarboxypeptidase A2. Deciphering the basis of its inhibition, activation and intrinsic activity of the zymogen EMBO J.. 13, 6906-6913 (1997).
    • (1997) EMBO J.. , vol.13 , pp. 6906-6913
    • Garcia-Sáez, I.1    Reverter, D.2    Vendrell, J.3    Aviles, F.X.4    Coll, M.5
  • 21
    • 0028282555 scopus 로고
    • Backbone dynamics of a free and a phosphopeptide-complexed Src homology 2. Study by 1SN NMR relaxation
    • Farrow N.A. et si. Backbone dynamics of a free and a phosphopeptide-complexed Src homology 2. Study by 1SN NMR relaxation. Biochemistry 33, 5984-6003 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1
  • 22
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity
    • Coll. M., Guasch, A., Aviles, FX. & Huber, R. Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. CMBO J. 10, 1-9 (1991).
    • (1991) CMBO J. , vol.10 , pp. 1-9
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 23
    • 0026782076 scopus 로고
    • Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris
    • Teplyakov, AV., et al. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris. Eur. J. Biochem. 208, 281-288 (1992).
    • (1992) Eur. J. Biochem. , vol.208 , pp. 281-288
    • Teplyakov, A.V.1
  • 24
    • 0029114209 scopus 로고
    • The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase a with proproteinase E and chymotrypsinogen C
    • Gomis-Ruth, FX., Gomez, M., Bode, W., Huber, R. & Aviles, F.X. The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C. EMBO J. 14, 4387-4394 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4387-4394
    • Gomis-Ruth, F.X.1    Gomez, M.2    Bode, W.3    Huber, R.4    Aviles, F.X.5
  • 26
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim, M., et al. Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb. Haemost. 78, 386-391 (1997).
    • (1997) Thromb. Haemost. , vol.78 , pp. 386-391
    • Nesheim, M.1
  • 27
    • 0032488932 scopus 로고    scopus 로고
    • Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway
    • Reverter, D., Ventura, S., Villegas, V., Vendrell, J. & Avilés, F.X. Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway. J. Biol. Chem. 273, 3535-3541 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3535-3541
    • Reverter, D.1    Ventura, S.2    Villegas, V.3    Vendrell, J.4    Avilés, F.X.5
  • 28
    • 0030965992 scopus 로고    scopus 로고
    • Toward antibody-directed enzyme prodrug therapy with the T268G mutant of human carboxypeptidase A1 and novel in vivo stable prodrugs of methotrexate
    • Smith, G.K., et al. Toward antibody-directed enzyme prodrug therapy with the T268G mutant of human carboxypeptidase A1 and novel in vivo stable prodrugs of methotrexate. J. Biol. Chem. 272, 15804-15816 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15804-15816
    • Smith, G.K.1
  • 30
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating-frame and isotropic mixing experiments
    • Ranee, M. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J. Magn. Reson. 74, 557-564 (1987).
    • (1987) J. Magn. Reson. , vol.74 , pp. 557-564
    • Ranee, M.1
  • 31
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meler, B.H., Bachman, P. & Ernst, R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553 (1979).
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meler, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 32
    • 5144233105 scopus 로고
    • MLEV-17-Based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax. A., Davis, D.G. MLEV-17-Based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360(1985).
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 33
    • 33747530131 scopus 로고    scopus 로고
    • An improved homonuclear TOCSY experiment with minimal water saturation
    • Dhalluin, C., Wieruszeki, J.M. & Lippens, G. An improved homonuclear TOCSY experiment with minimal water saturation. J. Magn. Reson. III 168-170 (1996).
    • (1996) J. Magn. Reson. , vol.3 , pp. 168-170
    • Dhalluin, C.1    Wieruszeki, J.M.2    Lippens, G.3
  • 34
    • 0024815191 scopus 로고
    • Determination of the complete 3-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. Determination of the complete 3-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).
    • (1989) J. Mol. Biol. , vol.210 , pp. 635-648
    • Holak, T.A.1    Gondol, D.2    Otlewski, J.3    Wilusz, T.4
  • 35
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim, Y. & Prestegard, J.H. Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84, 9-13 (1989).
    • (1989) J. Magn. Reson. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 36
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin C
    • Hyberts, S.G., Maki, W. & Wagner, G. Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin C. Eur. J. Biochem. 164, 625-635 (1987).
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Maki, W.2    Wagner, G.3
  • 38
    • 0026206788 scopus 로고
    • Sparse matrix sample: A screening method for crystallization of proteins
    • Jancarik, J. & Kim, S.H. Sparse matrix sample: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24,409-411 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 40
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza, J. AmoRe: an automated package for molecular replacement. Acta Crystallogr. A 50,157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 41
    • 0028103275 scopus 로고
    • CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50,760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 43
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., S Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296(1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.