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Volumn 19, Issue 3, 2009, Pages 226-231

Insulin-like growth factor-I (IGF-I): Solution properties and NMR chemical shift assignments near physiological pH

Author keywords

Assignment; Chemical shift; Insulin like growth factor; Nuclear magnetic resonance; Solution properties

Indexed keywords

CARBON 13; NITROGEN 15; SOMATOMEDIN C;

EID: 67349153102     PISSN: 10966374     EISSN: 15322238     Source Type: Journal    
DOI: 10.1016/j.ghir.2008.10.003     Document Type: Article
Times cited : (3)

References (42)
  • 3
    • 20744455262 scopus 로고    scopus 로고
    • IGF-binding proteins - the pieces are falling into place
    • Bach L.A., Headey S.J., and Norton R.S. IGF-binding proteins - the pieces are falling into place. Trends Endocrinol. Metab. 16 (2005) 228-234
    • (2005) Trends Endocrinol. Metab. , vol.16 , pp. 228-234
    • Bach, L.A.1    Headey, S.J.2    Norton, R.S.3
  • 4
    • 0036905115 scopus 로고    scopus 로고
    • Cellular actions of the insulin-like growth factor binding proteins
    • Firth S.M., and Baxter R.C. Cellular actions of the insulin-like growth factor binding proteins. Endocrinol. Rev. 23 (2002) 824-854
    • (2002) Endocrinol. Rev. , vol.23 , pp. 824-854
    • Firth, S.M.1    Baxter, R.C.2
  • 6
    • 18044386756 scopus 로고    scopus 로고
    • Insulin-like growth factor-I treatment of growth disorders, diabetes mellitus and insulin resistance
    • Ranke M.B. Insulin-like growth factor-I treatment of growth disorders, diabetes mellitus and insulin resistance. Trends Endocrinol. Metab. 16 (2005) 190-197
    • (2005) Trends Endocrinol. Metab. , vol.16 , pp. 190-197
    • Ranke, M.B.1
  • 7
    • 21344438173 scopus 로고    scopus 로고
    • Interaction of insulin-like growth factor (IGF)-I and -II with IGF binding protein-2: mapping the binding surfaces by nuclear magnetic resonance
    • Carrick F.E., Hinds M.G., McNeil K.A., Wallace J.C., Forbes B.E., and Norton R.S. Interaction of insulin-like growth factor (IGF)-I and -II with IGF binding protein-2: mapping the binding surfaces by nuclear magnetic resonance. J. Mol. Endocrinol. 34 (2005) 685-698
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 685-698
    • Carrick, F.E.1    Hinds, M.G.2    McNeil, K.A.3    Wallace, J.C.4    Forbes, B.E.5    Norton, R.S.6
  • 8
    • 0025822851 scopus 로고
    • Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
    • Cooke R.M., Harvey T.S., and Campbell I.D. Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study. Biochemistry 30 (1991) 5484-5491
    • (1991) Biochemistry , vol.30 , pp. 5484-5491
    • Cooke, R.M.1    Harvey, T.S.2    Campbell, I.D.3
  • 9
    • 2942596337 scopus 로고    scopus 로고
    • Binding site for the C-domain of insulin-like growth factor (IGF) binding protein-6 on IGF-II; implications for inhibition of IGF actions
    • Headey S.J., Keizer D.W., Yao S., Wallace J.C., Bach L.A., and Norton R.S. Binding site for the C-domain of insulin-like growth factor (IGF) binding protein-6 on IGF-II; implications for inhibition of IGF actions. FEBS Lett. 568 (2004) 19-22
    • (2004) FEBS Lett. , vol.568 , pp. 19-22
    • Headey, S.J.1    Keizer, D.W.2    Yao, S.3    Wallace, J.C.4    Bach, L.A.5    Norton, R.S.6
  • 10
    • 33748785712 scopus 로고    scopus 로고
    • The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state
    • Hua Q.X., Mayer J.P., Jia W., Zhang J., and Weiss M.A. The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state. J. Biol. Chem. 281 (2006) 28131-28142
    • (2006) J. Biol. Chem. , vol.281 , pp. 28131-28142
    • Hua, Q.X.1    Mayer, J.P.2    Jia, W.3    Zhang, J.4    Weiss, M.A.5
  • 11
    • 0032544407 scopus 로고    scopus 로고
    • The insulin-like growth factor (IGF) binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis
    • Jansson M., Andersson G., Uhlen M., Nilsson B., and Kordel J. The insulin-like growth factor (IGF) binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis. J. Biol. Chem. 273 (1998) 24701-24707
    • (1998) J. Biol. Chem. , vol.273 , pp. 24701-24707
    • Jansson, M.1    Andersson, G.2    Uhlen, M.3    Nilsson, B.4    Kordel, J.5
  • 13
    • 0034616133 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of long-[Arg(3)]-insulin-like growth factor-I
    • Laajoki L.G., Francis G.L., Wallace J.C., Carver J.A., and Keniry M.A. Solution structure and backbone dynamics of long-[Arg(3)]-insulin-like growth factor-I. J. Biol. Chem. 275 (2000) 10009-10015
    • (2000) J. Biol. Chem. , vol.275 , pp. 10009-10015
    • Laajoki, L.G.1    Francis, G.L.2    Wallace, J.C.3    Carver, J.A.4    Keniry, M.A.5
  • 15
    • 0041571486 scopus 로고    scopus 로고
    • Complex with a phage display-derived peptide provides insight into the function of insulin-like growth factor-I
    • Schaffer M.L., Deshayes K., Nakamura G., Sidhu S., and Skelton N.J. Complex with a phage display-derived peptide provides insight into the function of insulin-like growth factor-I. Biochemistry 42 (2003) 9324-9334
    • (2003) Biochemistry , vol.42 , pp. 9324-9334
    • Schaffer, M.L.1    Deshayes, K.2    Nakamura, G.3    Sidhu, S.4    Skelton, N.J.5
  • 16
    • 0028131962 scopus 로고
    • Solution structure of human insulin-like growth factor-II; recognition sites for receptors and binding proteins
    • Terasawa H., Kohda D., Hatanaka H., Nagata K., Higashihashi N., Fujiwara H., Sakano K., and Inagaki F. Solution structure of human insulin-like growth factor-II; recognition sites for receptors and binding proteins. EMBO J. 13 (1994) 5590-5597
    • (1994) EMBO J. , vol.13 , pp. 5590-5597
    • Terasawa, H.1    Kohda, D.2    Hatanaka, H.3    Nagata, K.4    Higashihashi, N.5    Fujiwara, H.6    Sakano, K.7    Inagaki, F.8
  • 17
    • 0029059589 scopus 로고
    • Solution structure of human insulin-like growth factor-II. Relationship to receptor and binding protein interactions
    • Torres A.M., Forbes B.E., Aplin S.E., Wallace J.C., Francis G.L., and Norton R.S. Solution structure of human insulin-like growth factor-II. Relationship to receptor and binding protein interactions. J. Mol. Biol. 248 (1995) 385-401
    • (1995) J. Mol. Biol. , vol.248 , pp. 385-401
    • Torres, A.M.1    Forbes, B.E.2    Aplin, S.E.3    Wallace, J.C.4    Francis, G.L.5    Norton, R.S.6
  • 18
    • 33751051488 scopus 로고    scopus 로고
    • Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2)
    • Kuang Z., Yao S., Keizer D.W., Wang C.C., Bach L.A., Forbes B.E., Wallace J.C., and Norton R.S. Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2). J. Mol. Biol. 364 (2006) 690-704
    • (2006) J. Mol. Biol. , vol.364 , pp. 690-704
    • Kuang, Z.1    Yao, S.2    Keizer, D.W.3    Wang, C.C.4    Bach, L.A.5    Forbes, B.E.6    Wallace, J.C.7    Norton, R.S.8
  • 19
    • 36849068849 scopus 로고    scopus 로고
    • Cooperativity of the N- and C-terminal domains of insulin-like growth factor (IGF) binding protein 2 in IGF binding
    • Kuang Z., Yao S., McNeil K.A., Thompson J.A., Bach L.A., Forbes B.E., Wallace J.C., and Norton R.S. Cooperativity of the N- and C-terminal domains of insulin-like growth factor (IGF) binding protein 2 in IGF binding. Biochemistry 46 (2007) 13720-13732
    • (2007) Biochemistry , vol.46 , pp. 13720-13732
    • Kuang, Z.1    Yao, S.2    McNeil, K.A.3    Thompson, J.A.4    Bach, L.A.5    Forbes, B.E.6    Wallace, J.C.7    Norton, R.S.8
  • 21
    • 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. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 22
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M., Schleucher J., and Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Progr. NMR Spectrosc. 34 (1999) 93-158
    • (1999) Progr. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 23
    • 0032694547 scopus 로고    scopus 로고
    • An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments
    • Diercks T., Coles M., and Kessler H. An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments. J. Biomol. NMR 15 (1999) 177-180
    • (1999) J. Biomol. NMR , vol.15 , pp. 177-180
    • Diercks, T.1    Coles, M.2    Kessler, H.3
  • 24
    • 46049109892 scopus 로고    scopus 로고
    • Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR
    • Yao S., Babon J.J., and Norton R.S. Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR. Biophys. Chem. 136 (2008) 145-151
    • (2008) Biophys. Chem. , vol.136 , pp. 145-151
    • Yao, S.1    Babon, J.J.2    Norton, R.S.3
  • 25
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins D.K., Grimshaw S.B., Receveur V., Dobson C.M., Jones J.A., and Smith L.J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38 (1999) 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 27
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • Garcia de la Torre J., Huertas M.L., and Carrasco B. HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. J. Magn. Reson. 147 (2000) 138-146
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 28
    • 0035909073 scopus 로고    scopus 로고
    • Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions
    • Vajdos F.F., Ultsch M., Schaffer M.L., Deshayes K.D., Liu J., Skelton N.J., and de Vos A.M. Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions. Biochemistry 40 (2001) 11022-11029
    • (2001) Biochemistry , vol.40 , pp. 11022-11029
    • Vajdos, F.F.1    Ultsch, M.2    Schaffer, M.L.3    Deshayes, K.D.4    Liu, J.5    Skelton, N.J.6    de Vos, A.M.7
  • 29
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri A.A., Hinton D.P., and Byrd R.A. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117 (1995) 7566-7567
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7566-7567
    • Altieri, A.A.1    Hinton, D.P.2    Byrd, R.A.3
  • 30
    • 0017368283 scopus 로고
    • 1H NMR titration shifts of amide proton resonances in polypeptide chains
    • 1H NMR titration shifts of amide proton resonances in polypeptide chains. FEBS Lett. 77 (1977) 11-14
    • (1977) FEBS Lett. , vol.77 , pp. 11-14
    • Bundi, A.1    Wüthrich, K.2
  • 32
    • 0015766825 scopus 로고
    • Carbon 13 nuclear magnetic resonance of pentapeptides of glycine containing central residues of serine, threonine, aspartic and glutamic acids, asparagine, and glutamine
    • Keim P., Vigna R.A., Morrow J.S., Marshall R.C., and Gurd F.R. Carbon 13 nuclear magnetic resonance of pentapeptides of glycine containing central residues of serine, threonine, aspartic and glutamic acids, asparagine, and glutamine. J. Biol. Chem. 248 (1973) 7811-7818
    • (1973) J. Biol. Chem. , vol.248 , pp. 7811-7818
    • Keim, P.1    Vigna, R.A.2    Morrow, J.S.3    Marshall, R.C.4    Gurd, F.R.5
  • 34
    • 0033619710 scopus 로고    scopus 로고
    • Insulin-like growth factor-I and its binding proteins: a study of the binding interface using B-domain analogues
    • Magee B.A., Shooter G.K., Wallace J.C., and Francis G.L. Insulin-like growth factor-I and its binding proteins: a study of the binding interface using B-domain analogues. Biochemistry 38 (1999) 15863-15870
    • (1999) Biochemistry , vol.38 , pp. 15863-15870
    • Magee, B.A.1    Shooter, G.K.2    Wallace, J.C.3    Francis, G.L.4
  • 36
    • 0036137007 scopus 로고    scopus 로고
    • A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix
    • Xu B., Hua Q.X., Nakagawa S.H., Jia W., Chu Y.C., Katsoyannis P.G., and Weiss M.A. A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix. Protein Sci. 11 (2002) 104-116
    • (2002) Protein Sci. , vol.11 , pp. 104-116
    • Xu, B.1    Hua, Q.X.2    Nakagawa, S.H.3    Jia, W.4    Chu, Y.C.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 37
    • 0037044828 scopus 로고    scopus 로고
    • Mechanism of insulin chain combination. Asymmetric roles of A-chain α-helices in disulfide pairing
    • Hua Q.X., Chu Y.C., Jia W., Phillips N.F., Wang R.Y., Katsoyannis P.G., and Weiss M.A. Mechanism of insulin chain combination. Asymmetric roles of A-chain α-helices in disulfide pairing. J. Biol. Chem. 277 (2002) 43443-43453
    • (2002) J. Biol. Chem. , vol.277 , pp. 43443-43453
    • Hua, Q.X.1    Chu, Y.C.2    Jia, W.3    Phillips, N.F.4    Wang, R.Y.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 38
    • 47249140371 scopus 로고    scopus 로고
    • Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications
    • Hua Q.X., Nakagawa S.H., Jia W., Huang K., Phillips N.B., Hu S.Q., and Weiss M.A. Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications. J. Biol. Chem. 283 (2008) 14703-14716
    • (2008) J. Biol. Chem. , vol.283 , pp. 14703-14716
    • Hua, Q.X.1    Nakagawa, S.H.2    Jia, W.3    Huang, K.4    Phillips, N.B.5    Hu, S.Q.6    Weiss, M.A.7
  • 39
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua Q.X., Shoelson S.E., Kochoyan M., and Weiss M.A. Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354 (1991) 238-241
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 40
    • 0038461955 scopus 로고    scopus 로고
    • Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils
    • Dong J., Wan Z., Popov M., Carey P.R., and Weiss M.A. Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils. J. Mol. Biol. 330 (2003) 431-442
    • (2003) J. Mol. Biol. , vol.330 , pp. 431-442
    • Dong, J.1    Wan, Z.2    Popov, M.3    Carey, P.R.4    Weiss, M.A.5
  • 41
    • 33747670241 scopus 로고    scopus 로고
    • Toward the active conformation of insulin: stereospecific modulation of a structural switch in the B chain
    • Hua Q.X., Nakagawa S., Hu S.Q., Jia W., Wang S., and Weiss M.A. Toward the active conformation of insulin: stereospecific modulation of a structural switch in the B chain. J. Biol. Chem. 281 (2006) 24900-24909
    • (2006) J. Biol. Chem. , vol.281 , pp. 24900-24909
    • Hua, Q.X.1    Nakagawa, S.2    Hu, S.Q.3    Jia, W.4    Wang, S.5    Weiss, M.A.6


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