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Volumn 47, Issue 50, 2008, Pages 13308-13317

Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CONFORMATIONS; HYDROGEN; HYDROGEN BONDS; PROTEIN FOLDING;

EID: 57649134244     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801412w     Document Type: Article
Times cited : (4)

References (64)
  • 2
    • 0018184054 scopus 로고
    • The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin
    • Rinderknecht, E., and Humbel, R. E. (1978) The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin. J. Biol. Chem. 253, 2769-2776.
    • (1978) J. Biol. Chem , vol.253 , pp. 2769-2776
    • Rinderknecht, E.1    Humbel, R.E.2
  • 3
    • 0017647633 scopus 로고
    • Relaxin: A disulfide homolog of insulin
    • Schwabe, C., and McDonald, J. K. (1977) Relaxin: A disulfide homolog of insulin. Science 197, 914-915.
    • (1977) Science , vol.197 , pp. 914-915
    • Schwabe, C.1    McDonald, J.K.2
  • 5
    • 0027365039 scopus 로고
    • Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells
    • Adham, I. M., Burkhardt, E., Benahmed, M., and Engel, W. (1993) Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells. J. Biol. Chem. 268, 26668-26672.
    • (1993) J. Biol. Chem , vol.268 , pp. 26668-26672
    • Adham, I.M.1    Burkhardt, E.2    Benahmed, M.3    Engel, W.4
  • 6
    • 0029095815 scopus 로고
    • Cloning of a new member of the insulin gene superfamily (INSL4) expressed in human placenta
    • Chassin, D., Laurent, A., Janneau, J. L., Berger, R., and Bellet, D. (1995) Cloning of a new member of the insulin gene superfamily (INSL4) expressed in human placenta. Genomics 29, 465-470.
    • (1995) Genomics , vol.29 , pp. 465-470
    • Chassin, D.1    Laurent, A.2    Janneau, J.L.3    Berger, R.4    Bellet, D.5
  • 8
    • 0034463049 scopus 로고    scopus 로고
    • Identification, chromosomal mapping, and partial characterization of mouse insl6: A new member of the insulin family
    • Kasik, J., Muglia, L., Stephan, D. A., and Menon, R. K. (2000) Identification, chromosomal mapping, and partial characterization of mouse insl6: A new member of the insulin family. Endocrinology 141, 458-461.
    • (2000) Endocrinology , vol.141 , pp. 458-461
    • Kasik, J.1    Muglia, L.2    Stephan, D.A.3    Menon, R.K.4
  • 13
    • 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. (1995) Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. J. Mol. Biol. 248, 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
  • 14
    • 0025812626 scopus 로고
    • X-ray structure of human relaxin at 1.5 Å: Comparison to insulin and implications for receptor binding determinants
    • Eigenbrot, C., Randal, M., Quan, C., Burnier, J., O'Connell, L., Rinderknecht, E., and Kossiakoff, A. A. (1991) X-ray structure of human relaxin at 1.5 Å: Comparison to insulin and implications for receptor binding determinants. J. Mol. Biol. 221, 15-21.
    • (1991) J. Mol. Biol , vol.221 , pp. 15-21
    • Eigenbrot, C.1    Randal, M.2    Quan, C.3    Burnier, J.4    O'Connell, L.5    Rinderknecht, E.6    Kossiakoff, A.A.7
  • 15
    • 33646832952 scopus 로고    scopus 로고
    • Solution structure and novel insight into determinants of receptor specificity of human relaxin-3
    • Rosengren, K. J., Lin, F., Bathgate, R. A. D., Tregear, G. W., Daly, N. L., Wade, J. D., and Craik, D. J. (2006) Solution structure and novel insight into determinants of receptor specificity of human relaxin-3. J. Biol. Chem. 281, 5845-5851.
    • (2006) J. Biol. Chem , vol.281 , pp. 5845-5851
    • Rosengren, K.J.1    Lin, F.2    Bathgate, R.A.D.3    Tregear, G.W.4    Daly, N.L.5    Wade, J.D.6    Craik, D.J.7
  • 23
    • 5644233835 scopus 로고    scopus 로고
    • Insulin-like 3 signalling in testicular descent
    • Adham, I. M., and Agoulnik, A. I. (2004) Insulin-like 3 signalling in testicular descent. Int. J. Androl. 27, 257-265.
    • (2004) Int. J. Androl , vol.27 , pp. 257-265
    • Adham, I.M.1    Agoulnik, A.I.2
  • 24
    • 0037039453 scopus 로고    scopus 로고
    • The primary structure and the disulfide links of the bovine relaxin-like factor (RLF)
    • Büllesbach, E. E., and Schwabe, C. (2002) The primary structure and the disulfide links of the bovine relaxin-like factor (RLF). Biochemistry 41, 274-281.
    • (2002) Biochemistry , vol.41 , pp. 274-281
    • Büllesbach, E.E.1    Schwabe, C.2
  • 25
    • 3042658646 scopus 로고    scopus 로고
    • Synthetic cross-links arrest the C-terminal region of the relaxin-like factor (RLF) in an active conformation
    • Büllesbach, E. E., and Schwabe, C. (2004) Synthetic cross-links arrest the C-terminal region of the relaxin-like factor (RLF) in an active conformation. Biochemistry 43, 8021-8028.
    • (2004) Biochemistry , vol.43 , pp. 8021-8028
    • Büllesbach, E.E.1    Schwabe, C.2
  • 28
    • 33748746259 scopus 로고    scopus 로고
    • The mode of interaction of the relaxin-like factor (RLF) with the leucine-rich repeat G protein-activated receptor 8
    • Büllesbach, E. E., and Schwabe, C. (2006) The mode of interaction of the relaxin-like factor (RLF) with the leucine-rich repeat G protein-activated receptor 8. J. Biol. Chem. 281, 26136-26143.
    • (2006) J. Biol. Chem , vol.281 , pp. 26136-26143
    • Büllesbach, E.E.1    Schwabe, C.2
  • 29
    • 0039613991 scopus 로고    scopus 로고
    • Tryptophan B27 in the relaxin-like factor (RLF) is crucial for RLF receptor binding
    • Büllesbach, E. E., and Schwabe, C. (1999) Tryptophan B27 in the relaxin-like factor (RLF) is crucial for RLF receptor binding. Biochemistry 38, 3073-3078.
    • (1999) Biochemistry , vol.38 , pp. 3073-3078
    • Büllesbach, E.E.1    Schwabe, C.2
  • 30
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 32
    • 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.
    • (1979) J. Chem. Phys , vol.71 , pp. 4546
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 33
    • 49049150378 scopus 로고
    • Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins
    • Macura, S., Huang, Y., Suter, D., and Ernst, R. R. (1981) Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43, 259-281.
    • (1981) J. Magn. Reson , vol.43 , pp. 259-281
    • Macura, S.1    Huang, Y.2    Suter, D.3    Ernst, R.R.4
  • 34
    • 0344448273 scopus 로고
    • Coherence transfer by isotopic mixing application to proton correlation spectroscopy
    • Braunschweiler, L., and Ernst, R. R. (1983) Coherence transfer by isotopic mixing application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 35
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 36
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 38
    • 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., and 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
  • 40
    • 0030208881 scopus 로고    scopus 로고
    • Estimation of signal intensities in 2D NMR spectra with severe basline distortion by combined linear-prediction and least-square analyses
    • Kristensen, S. M., Sørensen, M. D., Gesmar, H., and Led, J. J. (1996) Estimation of signal intensities in 2D NMR spectra with severe basline distortion by combined linear-prediction and least-square analyses. J. Magn. Reson., Ser. B 112, 193.
    • (1996) J. Magn. Reson., Ser. B , vol.112 , pp. 193
    • Kristensen, S.M.1    Sørensen, M.D.2    Gesmar, H.3    Led, J.J.4
  • 41
    • 33747831881 scopus 로고    scopus 로고
    • PREDITOR: A web server for predicting protein torsion angle restraints
    • Berjanskii, M. V., Neal, S., and Wishart, D. S. (2006) PREDITOR: A web server for predicting protein torsion angle restraints. Nucleic Acids Res. 34, W63-W69.
    • (2006) Nucleic Acids Res , vol.34
    • Berjanskii, M.V.1    Neal, S.2    Wishart, D.S.3
  • 42
    • 0002934112 scopus 로고
    • Structure determination from NMR data. I Analysis of NMR data
    • Roberts, G. C. K, Ed, pp, IRL Press, Oxford, U.K
    • Barsukov, I. L., and Lian, L. Y. (1993) Structure determination from NMR data. I Analysis of NMR data. In NMR of macromol ecules: A practical approach (Roberts, G. C. K., Ed.) pp 315-358, IRL Press, Oxford, U.K.
    • (1993) NMR of macromol ecules: A practical approach , pp. 315-358
    • Barsukov, I.L.1    Lian, L.Y.2
  • 43
    • 33847283016 scopus 로고    scopus 로고
    • ARIA2: Automated NOE assignment and data integration in NMR structure calculation
    • Rieping, W., Habeck, M., Bardiaux, B., Bernard, A., Malliavin, T. E., and Nilges, M. (2007) ARIA2: Automated NOE assignment and data integration in NMR structure calculation. Bioinformatics 23, 381-382.
    • (2007) Bioinformatics , vol.23 , pp. 381-382
    • Rieping, W.1    Habeck, M.2    Bardiaux, B.3    Bernard, A.4    Malliavin, T.E.5    Nilges, M.6
  • 46
    • 18044378198 scopus 로고    scopus 로고
    • Multiple binding sites revealed by interaction of relaxin family peptides with native and chimeric relaxin family peptide receptors 1 and 2 (LGR7 and LGR8)
    • Halls, M. L., Bond, C. P., Sudo, S., Kumagai, J., Ferraro, T., Layfield, S., Bathgate, R. A., and Summers, R. J. (2005) Multiple binding sites revealed by interaction of relaxin family peptides with native and chimeric relaxin family peptide receptors 1 and 2 (LGR7 and LGR8). J. Pharmacol. Exp. Ther. 313, 677-687.
    • (2005) J. Pharmacol. Exp. Ther , vol.313 , pp. 677-687
    • Halls, M.L.1    Bond, C.P.2    Sudo, S.3    Kumagai, J.4    Ferraro, T.5    Layfield, S.6    Bathgate, R.A.7    Summers, R.J.8
  • 48
    • 0025778802 scopus 로고
    • Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition
    • Hua, Q. X., and Weiss, M. A. (1991) Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry 30, 5505-5515.
    • (1991) Biochemistry , vol.30 , pp. 5505-5515
    • Hua, Q.X.1    Weiss, M.A.2
  • 49
    • 0030612301 scopus 로고    scopus 로고
    • Solution structures of the R6 human insulin hexamer
    • Chang, X., Jorgensen, A. M., Bardrum, P., and Led, J. J. (1997) Solution structures of the R6 human insulin hexamer. Biochemistry 36, 9409-9422.
    • (1997) Biochemistry , vol.36 , pp. 9409-9422
    • Chang, X.1    Jorgensen, A.M.2    Bardrum, P.3    Led, J.J.4
  • 51
    • 4444383210 scopus 로고    scopus 로고
    • A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer
    • Zoete, V., Meuwly, M., and Karplus, M. (2004) A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer. J. Mol. Biol. 342, 913-929.
    • (2004) J. Mol. Biol , vol.342 , pp. 913-929
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 52
    • 0024553746 scopus 로고
    • Role of the phenylalanine B24 side chain in directing insulin interaction with its receptor: Importance of main chain conformation
    • Mirmira, R. G., and Tager, H. S. (1989) Role of the phenylalanine B24 side chain in directing insulin interaction with its receptor: Importance of main chain conformation. J. Biol. Chem. 264, 6349-6354.
    • (1989) J. Biol. Chem , vol.264 , pp. 6349-6354
    • Mirmira, R.G.1    Tager, H.S.2
  • 54
    • 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. (1991) Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354, 238-241.
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 55
    • 0026549524 scopus 로고
    • Structure and dynamics of des-pentapeptide-insulin in solution: The molten-globule hypothesis
    • Hua, Q. X., Kochoyan, M., and Weiss, M. A. (1992) Structure and dynamics of des-pentapeptide-insulin in solution: The molten-globule hypothesis. Proc. Natl. Acad. Sci. U.S.A. 89, 2379-2383.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 2379-2383
    • Hua, Q.X.1    Kochoyan, M.2    Weiss, M.A.3
  • 56
    • 0029986510 scopus 로고    scopus 로고
    • Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant: Elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin
    • Jørgensen, A. M. M., Olsen, H. B., Baischmidt, P., and Led, J. J. (1996) Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant: Elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin. J. Mol. Biol. 257, 684-699.
    • (1996) J. Mol. Biol , vol.257 , pp. 684-699
    • Jørgensen, A.M.M.1    Olsen, H.B.2    Baischmidt, P.3    Led, J.J.4
  • 57
    • 0035807039 scopus 로고    scopus 로고
    • Flexibility and bioactivity of insulin: An NMR investigation of the solution structure and folding of an unusually flexible human insulin mutant with increased biological activity
    • Keller, D., Clausen, R., Josefsen, K., and Led, J. J. (2001) Flexibility and bioactivity of insulin: An NMR investigation of the solution structure and folding of an unusually flexible human insulin mutant with increased biological activity. Biochemistry 40, 10732-10740.
    • (2001) Biochemistry , vol.40 , pp. 10732-10740
    • Keller, D.1    Clausen, R.2    Josefsen, K.3    Led, J.J.4
  • 58
    • 33746828162 scopus 로고    scopus 로고
    • Chiral mutagenesis of insulin. Contribution of the B20-B23 β-turn to activity and stability
    • Nakagawa, S. H., Hua, Q. X., Hu, S. Q., Jia, W., Wang, S., Katsoyannis, P. G., and Weiss, M. A. (2006) Chiral mutagenesis of insulin. Contribution of the B20-B23 β-turn to activity and stability. J. Biol. Chem. 281, 22386-22396.
    • (2006) J. Biol. Chem , vol.281 , pp. 22386-22396
    • Nakagawa, S.H.1    Hua, Q.X.2    Hu, S.Q.3    Jia, W.4    Wang, S.5    Katsoyannis, P.G.6    Weiss, M.A.7
  • 60
    • 0017224874 scopus 로고
    • Site-site interactions among insulin receptors: Characterization of the negative cooperativity
    • De Meyts, P., Bianco, A. R., and Roth, J. (1976) Site-site interactions among insulin receptors: Characterization of the negative cooperativity. J. Biol. Chem. 251, 1877-1888.
    • (1976) J. Biol. Chem , vol.251 , pp. 1877-1888
    • De Meyts, P.1    Bianco, A.R.2    Roth, J.3
  • 61
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric, allosteric membrane receptors?
    • De Meyts, P. (2008) The insulin receptor: A prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 33, 376-384.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 64
    • 17144426920 scopus 로고    scopus 로고
    • The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7
    • Büllesbach, E. E., and Schwabe, C. (2005) The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7. J. Biol. Chem. 280, 14051-14056.
    • (2005) J. Biol. Chem , vol.280 , pp. 14051-14056
    • Büllesbach, E.E.1    Schwabe, C.2


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