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Volumn 12, Issue 2, 2003, Pages 296-305

NMR solution structure of the activation domain of human procarboxypeptidase A2

Author keywords

Activation mechanism; Hydrogen deuterium exchange; Nuclear magnetic resonance; Procarboxypeptidase; Protein stability; Protein structure

Indexed keywords

AMIDE; AMYLOID; CARBOXYPEPTIDASE A; CARBOXYPEPTIDASE B; ENZYME PRECURSOR; PROCARBOXYPEPTIDASE A2; UNCLASSIFIED DRUG;

EID: 0037305973     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0227303     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy. Application to NMR
    • Aue, W.P., Bertholdi, E., and Ernst. R.R. 1976. Two-dimensional spectroscopy. Application to NMR. J. Chem. Phys. 64: 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bertholdi, E.2    Ernst, R.R.3
  • 2
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L., and Englander, S.W. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17: 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 3
    • 0028067152 scopus 로고
    • Protein stability parameters measured by hydrogen exchange
    • 1994. Protein stability parameters measured by hydrogen exchange. Proteins 20: 4-14.
    • (1994) Proteins , vol.20 , pp. 4-14
  • 4
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T.-H., Billeter, M., Güntert, P., and Wüthrich, 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.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 5
    • 0010285919 scopus 로고
    • Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy
    • Bax, A. and Subramanian. J. 1986. Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy. J. Magn. Reson. 67: 565-570.
    • (1986) J. Magn. Reson. , vol.67 , pp. 565-570
    • Bax, A.1    Subramanian, J.2
  • 6
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. and Ruben, D.J. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69: 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 7
    • 0000221195 scopus 로고
    • Computer-optimised homonuclear TOCSY experiments with suppression of cross relaxation
    • Briand, J. and Ernst, R.R. 1991. Computer-optimised homonuclear TOCSY experiments with suppression of cross relaxation. Chem. Phys. Lett. 185: 276-285.
    • (1991) Chem. Phys. Lett. , vol.185 , pp. 276-285
    • Briand, J.1    Ernst, R.R.2
  • 8
    • 84985653913 scopus 로고
    • 1H NMR titration shifts for studies of polypeptide conformation
    • 1H NMR titration shifts for studies of polypeptide conformation. Biopolymers 18: 299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wüthrich, K.2
  • 9
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
    • Clarke, J. and Fersht, A.R. 1996. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold. Des. 1: 243-254.
    • (1996) Fold. Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 10
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity
    • Coll, M., Guasch, A., Aviles, F.X., and Huber, R. 1991. Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity. EMBO J. 10: 1-9.
    • (1991) EMBO J , vol.10 , pp. 1-9
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 11
    • 0000132887 scopus 로고
    • pH dependence of internal references
    • De Marco, A. 1977. pH dependence of internal references. J. Magn. Reson. 26: 527-528.
    • (1977) J. Magn. Reson. , vol.26 , pp. 527-528
    • De Marco, A.1
  • 12
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S.W. and Kallenbach, N.R. 1984. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16: 521-655.
    • (1984) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 15
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR
    • Forman-Kay, J.D., Clore, G.M., and Gronenborn, A.M. 1992. Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 31: 3442-3452.
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 16
    • 0040974381 scopus 로고    scopus 로고
    • The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of inhibition, activation and intrinsic activity of the zymogen
    • García-Sáez, I., Reverter, D., Vendrell, J., Aviles, F.X., and Coll, M. 1997. The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of inhibition, activation and intrinsic activity of the zymogen. EMBO J. 16: 6906-6913.
    • (1997) EMBO J , vol.16 , pp. 6906-6913
    • García-Sáez, I.1    Reverter, D.2    Vendrell, J.3    Aviles, F.X.4    Coll, M.5
  • 17
    • 0026548881 scopus 로고
    • Three-dimensional structure of porcine pancreatic procarboxypeptidase A
    • Guasch, A., Coll, M., Aviles, F.X., and Huber, R. 1992. Three-dimensional structure of porcine pancreatic procarboxypeptidase A. J. Mol. Biol. 224: 141-157.
    • (1992) J. Mol. Biol. , vol.224 , pp. 141-157
    • Guasch, A.1    Coll, M.2    Aviles, F.X.3    Huber, R.4
  • 18
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 19
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyse structural motifs in proteins
    • Hutchinson, E.G. and Thornton, J.M. 1996. PROMOTIF - A program to identify and analyse structural motifs in proteins. Protein Sci. 5: 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 20
    • 0032876680 scopus 로고    scopus 로고
    • Protein conformational stabilities can be determined from hydrogen exchange rates
    • Huyghues-Despointes, B.M.P., Scholtz, J.M., and Pace, C.N. 1999. Protein conformational stabilities can be determined from hydrogen exchange rates. Nat. Struct. Biol. 6: 910-912.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 910-912
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Pace, C.N.3
  • 21
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. and Nielsen, S.O. 1966. Hydrogen exchange in proteins. Adv. Protein Chem, 21: 287-386.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 22
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts, G.S., Golberg, M.S., Havel, T.F., and Wagner, G. 1992. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci. 1: 736-751.
    • (1992) Protein Sci. , vol.1 , pp. 736-751
    • Hyberts, G.S.1    Golberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 23
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P., and Ernst, R.R. 1979, Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71: 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 24
    • 0028943576 scopus 로고
    • Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia coli hioredoxin
    • Jeng, M.F. and Dyson, H.J. 1995. Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia coli hioredoxin. Biochemistry 34: 611-619.
    • (1995) Biochemistry , vol.34 , pp. 611-619
    • Jeng, M.F.1    Dyson, H.J.2
  • 25
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R.R., and Wüthrich, K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95: 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 26
    • 0031583471 scopus 로고    scopus 로고
    • Amide hydrogen exchange and internal dynamics in the chemotactic protein CheY from Escherichia coli
    • Lacroix, E., Bruix, M., Löpez-Hernández, E., Serrano, L., and Rico, M. 1997. Amide hydrogen exchange and internal dynamics in the chemotactic protein CheY from Escherichia coli. J. Mol. Biol. 271: 472-487.
    • (1997) J. Mol. Biol. , vol.271 , pp. 472-487
    • Lacroix, E.1    Bruix, M.2    Löpez-Hernández, E.3    Serrano, L.4    Rico, M.5
  • 29
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy in aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single quantum NMR spectroscopy in aqueous solutions. J. Biomol. NMR 6: 661-665.
    • (1992) J. Biomol. NMR , vol.6 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 30
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating frame and isotropic mixing experiments
    • Rance, M. 1987. Improved techniques for homonuclear rotating frame and isotropic mixing experiments. J. Magn. Reson. 74: 557-564.
    • (1987) J. Magn. Reson. , vol.74 , pp. 557-564
    • Rance, M.1
  • 31
    • 49549146155 scopus 로고
    • Quadrature Fourier NMR detection: Simple multiplex for dual detection
    • Redfield, A.G. and Kuntz, S.D. 1975. Quadrature Fourier NMR detection: Simple multiplex for dual detection. J. Magn. Reson. 19: 250-254.
    • (1975) J. Magn. Reson. , vol.19 , pp. 250-254
    • Redfield, A.G.1    Kuntz, S.D.2
  • 32
    • 0032488932 scopus 로고    scopus 로고
    • Human procarboxypeptidase A2: Overexpression in Pichia pastoris and detailed characterization of its activation pathway
    • Reverter, D., Ventura, S., Villegas, V., Vendrell, J., and Aviles, F.X. 1998. Human procarboxypeptidase A2: Overexpression in Pichia pastoris and detailed characterization of its activation pathway. J. Biol. Chem. 273: 3535-3541.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3535-3541
    • Reverter, D.1    Ventura, S.2    Villegas, V.3    Vendrell, J.4    Aviles, F.X.5
  • 34
    • 0025255168 scopus 로고
    • The tryptic activation pathway of monomeric procarboxypeptidase A
    • Vendrell, J., Cuchillo, C.M., and Aviles, F.X. 1990. The tryptic activation pathway of monomeric procarboxypeptidase A. J. Biol. Chem. 256: 6949-6953.
    • (1990) J. Biol. Chem. , vol.256 , pp. 6949-6953
    • Vendrell, J.1    Cuchillo, C.M.2    Aviles, F.X.3
  • 35
    • 0026078012 scopus 로고
    • The NMR structure of the activation domain isolated from porcine procarboxypeptidase B
    • Vendrell, J., Billeter, M., Wider, G., Aviles, F.X., and Wüthrich, K. 1991. The NMR structure of the activation domain isolated from porcine procarboxypeptidase B. EMBO J. 10: 11-15.
    • (1991) EMBO J , vol.10 , pp. 11-15
    • Vendrell, J.1    Billeter, M.2    Wider, G.3    Aviles, F.X.4    Wüthrich, K.5
  • 36
    • 0034615567 scopus 로고    scopus 로고
    • Metallocarboxypeptidases and their potent inhibitors. Structure, funtion and biomedical properties
    • Vendrell, J., Querol, E., and Aviles, F.X. 2000. Metallocarboxypeptidases and their potent inhibitors. Structure, funtion and biomedical properties. Biochim. Biophys. Acta 1477: 284-298.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 284-298
    • Vendrell, J.1    Querol, E.2    Aviles, F.X.3
  • 37
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • Viguera, A.R., Villegas, V., Aviles, F.X., and Serrano, L. 1996. Favourable native-like helical local interactions can accelerate protein folding. Fold. Des. 2: 23-33.
    • (1996) Fold. Des. , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Aviles, F.X.3    Serrano, L.4
  • 38
    • 0034697104 scopus 로고    scopus 로고
    • Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins
    • Villanueva, J., Canals, F., Villegas, V., Querol, E., and Aviles, F.X. 2000. Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins. FEBS Lett. 472: 27-33.
    • (2000) FEBS Lett. , vol.472 , pp. 27-33
    • Villanueva, J.1    Canals, F.2    Villegas, V.3    Querol, E.4    Aviles, F.X.5
  • 39
    • 0028788480 scopus 로고
    • Evidence for a two-state folding transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas, V., Azuaga, A., Catasús, L., Reverter, D., Mateo, P.L., Aviles, F.X., and Serrano, L. 1995a. Evidence for a two-state folding transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 34: 15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasús, L.3    Reverter, D.4    Mateo, P.L.5    Aviles, F.X.6    Serrano, L.7
  • 40
    • 0029160572 scopus 로고
    • The activation pathway of Procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic process
    • Villegas, V., Vendrell, J., and Aviles, F.X. 1995b. The activation pathway of Procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic process. Protein Sci. 4: 1792-1800.
    • (1995) Protein Sci. , vol.4 , pp. 1792-1800
    • Villegas, V.1    Vendrell, J.2    Aviles, F.X.3
  • 41
    • 0030334742 scopus 로고
    • Stabilisation of proteins by rational design of α-helix stability using helix/coil transition theory
    • Villegas, V., Viguera, A.R., Aviles, F.X., and Serrano, L. 1995c. Stabilisation of proteins by rational design of α-helix stability using helix/coil transition theory. Fold. Des. 1: 29-34.
    • (1995) Fold. Des. , vol.1 , pp. 29-34
    • Villegas, V.1    Viguera, A.R.2    Aviles, F.X.3    Serrano, L.4
  • 42
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • Villegas, V., Martínez, J.C., Aviles, F.X., and Serrano, L. 1998. Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283: 1027-1036.
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martínez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 44
    • 0018782123 scopus 로고
    • Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor
    • Wagner, G. and Wüthrich, K. 1979. Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130: 31-37.
    • (1979) J. Mol. Biol. , vol.130 , pp. 31-37
    • Wagner, G.1    Wüthrich, K.2
  • 45
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbor effects. J. Biomol. NMR 5: 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 46
    • 0028140319 scopus 로고
    • Hydrogen exchanges rates and protein folding
    • Woodward, C.K. 1994. Hydrogen exchanges rates and protein folding. Curr. Opin. Struct. Biol. 4: 112-116.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 112-116
    • Woodward, C.K.1


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