메뉴 건너뛰기




Volumn 250, Issue 3, 1997, Pages 712-726

Three dimensional solution structure of human angiogenin determined by 1H,15N-NMR spectroscopy. Characterisation of histidine protonation states and pK(a) values

Author keywords

Angiogenesis; Histidine low pK(a); Histidine protonation; NMR; Protein structure; Ribonuclease

Indexed keywords

ANGIOGENIN; HISTIDINE; RIBONUCLEASE A;

EID: 0031574074     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00712.x     Document Type: Article
Times cited : (40)

References (60)
  • 1
    • 0028262928 scopus 로고
    • Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease
    • Acharya, K. R., Shapiro, R., Allen, S. C., Riordan, J. F. & Vallee, B. L. (1994) Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease, Proc. Natl Acad. Sci. USA 91, 2915-2919.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2915-2919
    • Acharya, K.R.1    Shapiro, R.2    Allen, S.C.3    Riordan, J.F.4    Vallee, B.L.5
  • 4
    • 0008011643 scopus 로고
    • Structure, properties and molecular evolution of pancreatic-type ribonucleases
    • Beintema, J. J. (1987) Structure, properties and molecular evolution of pancreatic-type ribonucleases, Life Chem. Rep. 4, 333-389.
    • (1987) Life Chem. Rep. , vol.4 , pp. 333-389
    • Beintema, J.J.1
  • 6
    • 0001603840 scopus 로고
    • Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2
    • Bicknell, R. & Vallee, B. L. (1989) Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2, Proc. Natl Acad. Sci. USA 86, 1573-1577.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 1573-1577
    • Bicknell, R.1    Vallee, B.L.2
  • 7
    • 0027468848 scopus 로고
    • Characterization and sequencing of rabbit, pig and mouse angiogenins: Discernment of functionally important residues and regions
    • Bond, M. D., Strydom, D. J. & Vallee, B. L. (1993) Characterization and sequencing of rabbit, pig and mouse angiogenins: discernment of functionally important residues and regions, Biochim. Biophys. Acta 1162, 177-186.
    • (1993) Biochim. Biophys. Acta , vol.1162 , pp. 177-186
    • Bond, M.D.1    Strydom, D.J.2    Vallee, B.L.3
  • 8
    • 0001709899 scopus 로고
    • Ribonuclease A: Least-squares refinement of structure at 1.45 Å resolution
    • Borkakoti, N., Moss, D. S. & Palmer, R. A. (1982) Ribonuclease A: least-squares refinement of structure at 1.45 Å resolution, Acta Crystallogr. Sect. B 38, 2210-2217.
    • (1982) Acta Crystallogr. Sect. B , vol.38 , pp. 2210-2217
    • Borkakoti, N.1    Moss, D.S.2    Palmer, R.A.3
  • 11
    • 33748476849 scopus 로고
    • Suppression of cross-relaxation effects in TOCSY spectra via a modified D1PSI-2 mixing sequence
    • Cavanagh, J. & Rance, M. (1992) Suppression of cross-relaxation effects in TOCSY spectra via a modified D1PSI-2 mixing sequence, J. Magn. Reson. 96, 670-678.
    • (1992) J. Magn. Reson. , vol.96 , pp. 670-678
    • Cavanagh, J.1    Rance, M.2
  • 12
    • 0023232748 scopus 로고
    • Chemical synthesis of a gene coding for human angiogenin, its expression in Escherichia coli and conversion of the product into its active form
    • Denèfle, P., Kovarik, S., Guitton, J.-D., Cartwright, T. & Mayaux, J.-F. (1987) Chemical synthesis of a gene coding for human angiogenin, its expression in Escherichia coli and conversion of the product into its active form, Gene 56, 61-70.
    • (1987) Gene , vol.56 , pp. 61-70
    • Denèfle, P.1    Kovarik, S.2    Guitton, J.-D.3    Cartwright, T.4    Mayaux, J.-F.5
  • 13
    • 0030037085 scopus 로고    scopus 로고
    • Contribution of a tyrosine side chain to ribonuclease A catalysis and stability
    • Eberhardt, E. S., Wittmayer, P. K., Templer, B. M. & Raines, R. T. (1996) Contribution of a tyrosine side chain to ribonuclease A catalysis and stability, Protein Sci. 5, 1697-1703.
    • (1996) Protein Sci. , vol.5 , pp. 1697-1703
    • Eberhardt, E.S.1    Wittmayer, P.K.2    Templer, B.M.3    Raines, R.T.4
  • 14
    • 77957224996 scopus 로고
    • (Neuberger, A. & Brocklehurst, K., eds) Elsevier Science Publishers, Amsterdam
    • Eftink, M. R. & Biltonen, R. L. (1987) in Hydrolytic enzymes (Neuberger, A. & Brocklehurst, K., eds) pp. 333-376, Elsevier Science Publishers, Amsterdam.
    • (1987) Hydrolytic Enzymes , pp. 333-376
    • Eftink, M.R.1    Biltonen, R.L.2
  • 18
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert, P. & Wüthrich, K. (1991) Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints, J. Biomol. NMR 1, 447-456.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 19
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 20
    • 0026059740 scopus 로고
    • Dual site model for the organogenic activity of angiogenin
    • Hallahan, T. W., Shapiro, R. & Vallee, B. L. (1991) Dual site model for the organogenic activity of angiogenin, Proc. Natl Acad. Sci. USA 88, 2222-2226.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2222-2226
    • Hallahan, T.W.1    Shapiro, R.2    Vallee, B.L.3
  • 21
    • 0026656238 scopus 로고
    • Importance of asparagine-61 and asparagine-109 to the angiogenic activity of human angiogenin
    • Hallahan, T. W., Shapiro, R., Strydom, D. J. & Vallee, B. L. (1992) Importance of asparagine-61 and asparagine-109 to the angiogenic activity of human angiogenin, Biochemistry 31, 8022-8029.
    • (1992) Biochemistry , vol.31 , pp. 8022-8029
    • Hallahan, T.W.1    Shapiro, R.2    Strydom, D.J.3    Vallee, B.L.4
  • 22
    • 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. & 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
  • 23
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R. & Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 25
    • 0026858537 scopus 로고
    • Positive φ-angles in proteins by nuclear magnetic resonance spectroscopy
    • Ludvigsen, S. & Poulsen, F. M. (1992) Positive φ-angles in proteins by nuclear magnetic resonance spectroscopy, J. Biomol. NMR 2, 227-233.
    • (1992) J. Biomol. NMR , vol.2 , pp. 227-233
    • Ludvigsen, S.1    Poulsen, F.M.2
  • 26
    • 0027445544 scopus 로고
    • Conformational analysis of protein structures derived from NMR data
    • MacArthur, M. W. & Thornton, J. M. (1993) Conformational analysis of protein structures derived from NMR data. Proteins 17, 232-251.
    • (1993) Proteins , vol.17 , pp. 232-251
    • MacArthur, M.W.1    Thornton, J.M.2
  • 28
    • 0000144365 scopus 로고
    • Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data
    • Marion, D. & Bax, A. (1989) Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data, J. Magn. Reson. 83, 205-211.
    • (1989) J. Magn. Reson. , vol.83 , pp. 205-211
    • Marion, D.1    Bax, A.2
  • 30
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R. & Bax, A. (1989b) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 31
    • 0016754174 scopus 로고
    • Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119
    • Markley, J. L. & Finkenstadt, W. R. (1975) Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119, Biochemistry 14, 3562-3566.
    • (1975) Biochemistry , vol.14 , pp. 3562-3566
    • Markley, J.L.1    Finkenstadt, W.R.2
  • 32
    • 0028262977 scopus 로고
    • Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity
    • Moroianu, J. & Riordan, J. F. (1994a) Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity, Proc. Natl Acad. Sci. USA 91, 1677-1681.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1677-1681
    • Moroianu, J.1    Riordan, J.F.2
  • 33
    • 0027941844 scopus 로고
    • Identification of the nucleolar targeting signal of human angiogenin
    • Moroianu, J. & Riordan, J. F. (1994b) Identification of the nucleolar targeting signal of human angiogenin, Biochem. Biophys. Res. Commun. 203, 1765-1772.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1765-1772
    • Moroianu, J.1    Riordan, J.F.2
  • 34
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges, M., Clore, G. M. & Gronenborn, A. M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations, FEBS Lett. 229, 317-324.
    • (1988) FEBS Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 36
    • 0027456412 scopus 로고
    • Glc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • Glc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques, Protein Sci. 2, 543-548.
    • (1993) Protein Sci. , vol.2 , pp. 543-548
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 37
    • 33845555707 scopus 로고
    • Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences
    • Plateau, P. & Guéron, M. (1982) Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences, J. Am. Chem. Soc. 104, 7310-7311.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Plateau, P.1    Guéron, M.2
  • 38
    • 0000477505 scopus 로고    scopus 로고
    • Gifa V. 4: A complete package for NMR data set processing
    • Pons, J.-L., Malliavin, T. E. & Delsuc, M.-A. (1996) Gifa V. 4: a complete package for NMR data set processing, J. Biomol. NMR 8, 445-452.
    • (1996) J. Biomol. NMR , vol.8 , pp. 445-452
    • Pons, J.-L.1    Malliavin, T.E.2    Delsuc, M.-A.3
  • 42
    • 0000915667 scopus 로고
    • The use of classification in baseline correction of FT NMR spectra
    • Rouh, A., Delsuc, M.-A., Bertrand, G. & Lallemand, J.-Y. (1993) The use of classification in baseline correction of FT NMR spectra, J. Magn. Reson. 102, 357-359.
    • (1993) J. Magn. Reson. , vol.102 , pp. 357-359
    • Rouh, A.1    Delsuc, M.-A.2    Bertrand, G.3    Lallemand, J.-Y.4
  • 44
  • 45
    • 0027511809 scopus 로고
    • High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy
    • Santoro, J., Gonzalez, C., Bruix, M., Neira, J. L., Nieto, J. L., Herranz, J. & Rico, M. (1993) High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy, J. Mol. Biol. 229, 722-734.
    • (1993) J. Mol. Biol. , vol.229 , pp. 722-734
    • Santoro, J.1    Gonzalez, C.2    Bruix, M.3    Neira, J.L.4    Nieto, J.L.5    Herranz, J.6    Rico, M.7
  • 46
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A. J., Barker, P. B. & Freeman, R. (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation, J. Magn. Reson. 64, 547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 47
    • 0022497178 scopus 로고
    • Characteristic ribonucleolytic activity of human angiogenin
    • Shapiro, R., Riordan, J. F. & Vallee, B. L. (1986) Characteristic ribonucleolytic activity of human angiogenin, Biochemistry 25, 3527-3532.
    • (1986) Biochemistry , vol.25 , pp. 3527-3532
    • Shapiro, R.1    Riordan, J.F.2    Vallee, B.L.3
  • 48
  • 49
    • 0024435026 scopus 로고
    • Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis
    • Shapiro, R. & Vallee, B. L. (1989) Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis, Biochemistry 28, 7401-7408.
    • (1989) Biochemistry , vol.28 , pp. 7401-7408
    • Shapiro, R.1    Vallee, B.L.2
  • 50
    • 0024522906 scopus 로고
    • Role of lysines in human angiogenin: Chemical modification and site-directed mutagenesis
    • Shapiro, R., Fox, E. A. & Riordan, J. F. (1989) Role of lysines in human angiogenin: chemical modification and site-directed mutagenesis, Biochemistry 28, 1726-1732.
    • (1989) Biochemistry , vol.28 , pp. 1726-1732
    • Shapiro, R.1    Fox, E.A.2    Riordan, J.F.3
  • 52
    • 0026589835 scopus 로고
    • Angiogenin supports endothelial and fibroblast cell adhesion
    • Soncin, F. (1992) Angiogenin supports endothelial and fibroblast cell adhesion, Proc. Natl Acad. Sci. USA 89, 2232-2236.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2232-2236
    • Soncin, F.1
  • 53
    • 0027275026 scopus 로고
    • 15N-1H correlation spectroscopy with spin-echo and gradient pulses
    • 15N-1H correlation spectroscopy with spin-echo and gradient pulses, FEBS Lett. 327, 261-264.
    • (1993) FEBS Lett. , vol.327 , pp. 261-264
    • Szewczak, A.A.1    Kellogg, G.W.2    Moore, P.B.3
  • 54
    • 0028045937 scopus 로고
    • Inhibition of degranulation of polymorphonuclear leukocytes by angiogenin and its tryptic fragment
    • Tschesche, H., Kopp, C., Hörl, W. H. & Hempelmann, U. (1994) Inhibition of degranulation of polymorphonuclear leukocytes by angiogenin and its tryptic fragment, J. Biol. Chem. 269, 30274-30280.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30274-30280
    • Tschesche, H.1    Kopp, C.2    Hörl, W.H.3    Hempelmann, U.4
  • 57
    • 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
  • 58
    • 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
  • 59
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonucleuse A refined at 1.26 Å
    • Wlodawer, A., Svensson, L. A., Sjölin, L. & Gilliland, G. L. (1988) Structure of phosphate-free ribonucleuse A refined at 1.26 Å, Biochemistry 27, 2705-2717.
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjölin, L.3    Gilliland, G.L.4
  • 60
    • 0028564999 scopus 로고
    • The structures of RNase A complexed with 3́-CMP and d(CpA): Active site conformation and conserved water molecules
    • Zegers, I., Maes, D., Dao-Thi, M.-H., Poortmans, F. Palmer, R. & Wyns, L. (1994) The structures of RNase A complexed with 3́-CMP and d(CpA): active site conformation and conserved water molecules, Protein Sci. 3, 2322-2339.
    • (1994) Protein Sci. , vol.3 , pp. 2322-2339
    • Zegers, I.1    Maes, D.2    Dao-Thi, M.-H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.