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Volumn 45, Issue 3, 2006, Pages 727-737

Determinants of cooperativity and site selectivity in human ileal bile acid binding protein

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; ENTHALPY; ISOTHERMS; LIPIDS; MOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TITRATION;

EID: 31044447930     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051781p     Document Type: Article
Times cited : (51)

References (35)
  • 1
    • 0028896925 scopus 로고
    • Cytoplasmic fatty acid-binding proteins: Their structure and genes
    • Veerkamp, J. H., and Maatman, R. G. (1995) Cytoplasmic fatty acid-binding proteins: Their structure and genes, Prog. Lipid Res. 34, 17-52.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.G.2
  • 2
    • 0030239495 scopus 로고    scopus 로고
    • Cellular fatty acid-binding proteins: Their function and physiological significance
    • Glatz, J. F., and van der Vusse, G. J. (1996) Cellular fatty acid-binding proteins: Their function and physiological significance, Prog. Lipid Res. 35, 243-282.
    • (1996) Prog. Lipid Res. , vol.35 , pp. 243-282
    • Glatz, J.F.1    Van Der Vusse, G.J.2
  • 3
    • 0025140903 scopus 로고
    • Identification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes
    • Lin, M. C., Kramer, W., and Wilson, F. A. (1990) Identification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes, J. Biol. Chem. 265, 14986-14995.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14986-14995
    • Lin, M.C.1    Kramer, W.2    Wilson, F.A.3
  • 4
    • 0025132671 scopus 로고
    • Developmental and structural studies of an intracellular lipid binding protein expressed in the ileal epithelium
    • Sacchettini, J. C., Hauft, S. M., van Camp, S. L., Cistola, D. P., and Gordon, J. I. (1990) Developmental and structural studies of an intracellular lipid binding protein expressed in the ileal epithelium, J. Biol. Chem. 265, 19199-19207.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19199-19207
    • Sacchettini, J.C.1    Hauft, S.M.2    Van Camp, S.L.3    Cistola, D.P.4    Gordon, J.I.5
  • 5
    • 0027282014 scopus 로고
    • Titration calorimetry as a binding assay for lipid-binding proteins
    • Miller, K. R., and Cistola, D. P. (1993) Titration calorimetry as a binding assay for lipid-binding proteins, Mol. Cell. Biochem. 123, 29-37.
    • (1993) Mol. Cell. Biochem. , vol.123 , pp. 29-37
    • Miller, K.R.1    Cistola, D.P.2
  • 8
    • 0141988886 scopus 로고    scopus 로고
    • Steroid ring hydroxylation patterns govern cooperativity in human bile acid binding protein
    • Tochtrop, G. P., Bruns, J. M., Tang, C., Covey, D. F, and Cistola, D. P. (2003) Steroid ring hydroxylation patterns govern cooperativity in human bile acid binding protein, Biochemistry 42, 11561-11567.
    • (2003) Biochemistry , vol.42 , pp. 11561-11567
    • Tochtrop, G.P.1    Bruns, J.M.2    Tang, C.3    Covey, D.F.4    Cistola, D.P.5
  • 9
    • 4444375054 scopus 로고    scopus 로고
    • A single hydroxyl group governs ligand site selectivity in human ileal bile acid binding protein
    • Tochtrop, G. P., DeKoster, G. T., Covey, D. F., and Cistola, D. P. (2004) A single hydroxyl group governs ligand site selectivity in human ileal bile acid binding protein, J. Am. Chem. Soc. 126, 11024-11029.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11024-11029
    • Tochtrop, G.P.1    Dekoster, G.T.2    Covey, D.F.3    Cistola, D.P.4
  • 10
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B., and Saiki, R. K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions, Nucleic Acid Res. 16, 7351-7367.
    • (1988) Nucleic Acid Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 11
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. D., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.D.3    Pullen, J.K.4    Pease, L.R.5
  • 12
    • 0029367113 scopus 로고
    • 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein
    • 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein, J. Biomol. NMR 6, 198-210.
    • (1995) J. Biomol. NMR , vol.6 , pp. 198-210
    • Hodsdon, M.E.1    Toner, J.J.2    Cistola, D.P.3
  • 13
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing
    • Johnson, B. H., and Hecht, M. H. (1994) Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing, Biotechnology 12, 1357-1360.
    • (1994) Biotechnology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 14
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 15
    • 0017401311 scopus 로고
    • An improved procedure for the synthesis of glycine and taurine conjugates of bile salts
    • Tserng, K. Y., Hachey, D. L., and Klein, P. D. (1977) An improved procedure for the synthesis of glycine and taurine conjugates of bile salts, J. Lipid Res. 18, 404-407.
    • (1977) J. Lipid Res. , vol.18 , pp. 404-407
    • Tserng, K.Y.1    Hachey, D.L.2    Klein, P.D.3
  • 16
    • 43949167657 scopus 로고
    • HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- and β-carbon resonances in proteins
    • Wittekind, M., and Mueller, L. (1993) HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- and β-carbon resonances in proteins, J. Magn. Res. B 101, 201-205.
    • (1993) J. Magn. Res. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 17
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhindaram, D. R., and Kay, L. E. (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity, J. Magn. Res. B 103, 203-216.
    • (1994) J. Magn. Res. B , vol.103 , pp. 203-216
    • Muhindaram, D.R.1    Kay, L.E.2
  • 19
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S., and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR, J. Am. Chem. Soc. 114, 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 20
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • Ikura, M., Kay, L. E., and Bax, A. (1990) A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin, Biochemistry 29, 4659-4667.
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 21
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek, S., and Bax, A. (1992) Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein, J. Magn. Res. 96, 432-440.
    • (1992) J. Magn. Res. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 22
    • 0001498267 scopus 로고
    • 1Ha chemical shifts in uniformly carbon-13-labeled proteins dissolved in water
    • 1Ha chemical shifts in uniformly carbon-13-labeled proteins dissolved in water, J. Am. Chem. Soc. 115, 2055-2057.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2055-2057
    • Kay, L.E.1
  • 24
    • 44949269615 scopus 로고
    • A gradient enhanced HCCH-TOCSY experiment for recording side-chain proton and carbon-13 correlations in water samples of proteins
    • Kay, L. E., Xu, G. Y., Singer, A. U., Muhandiram, D. R., and Forman-Kay, J. D. (1993) A gradient enhanced HCCH-TOCSY experiment for recording side-chain proton and carbon-13 correlations in water samples of proteins, J. Magn. Res. B 101, 333-337.
    • (1993) J. Magn. Res. B , vol.101 , pp. 333-337
    • Kay, L.E.1    Xu, G.Y.2    Singer, A.U.3    Muhandiram, D.R.4    Forman-Kay, J.D.5
  • 26
    • 0025924784 scopus 로고
    • 13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: Application to interleukin 1 β
    • 13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: Application to interleukin 1 β, Biochemistry 30, 12-18.
    • (1991) Biochemistry , vol.30 , pp. 12-18
    • Clore, G.M.1    Kay, L.E.2    Bax, A.3    Gronenborn, A.M.4
  • 27
    • 0031064317 scopus 로고    scopus 로고
    • Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
    • Zhang, O., Forman-Kay, J. D., Shortle, D., and Kay, L. E. (1997) Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins, J. Biomol. NMR 9, 181-200.
    • (1997) J. Biomol. NMR , vol.9 , pp. 181-200
    • Zhang, O.1    Forman-Kay, J.D.2    Shortle, D.3    Kay, L.E.4
  • 28
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 29
    • 44049117096 scopus 로고
    • Effective combination of gradients and crafted RF pulses for water suppression in biological samples
    • John, B. K., Plant, D., Webb, P., and Hurd, R. E. (1992) Effective combination of gradients and crafted RF pulses for water suppression in biological samples, J. Magn. Res. 98, 200-206.
    • (1992) J. Magn. Res. , vol.98 , pp. 200-206
    • John, B.K.1    Plant, D.2    Webb, P.3    Hurd, R.E.4
  • 30
    • 0028393784 scopus 로고
    • 13C chemical shift index: A simple method for the identification of protein secondary structure using chemical shift data
    • 13C chemical shift index: A simple method for the identification of protein secondary structure using chemical shift data, J. Biomol. NMR 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 31
    • 0242652220 scopus 로고    scopus 로고
    • Solution structure of ileal lipid binding protein in complex with glycocholate
    • Lücke, C., Zhang, F., Hamilton, J. A., Sacchettini, J. C., and Rüterjans, H. (2000) Solution structure of ileal lipid binding protein in complex with glycocholate, Eur. J. Biochem. 267, 2929-2938.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2929-2938
    • Lücke, C.1    Zhang, F.2    Hamilton, J.A.3    Sacchettini, J.C.4    Rüterjans, H.5
  • 32
    • 33947332551 scopus 로고
    • On the refractive indices of aqueous solutions of urea
    • Warren, J. R., and Gordon, J. A. (1966) On the refractive indices of aqueous solutions of urea, J. Phys. Chem. 70, 297-300.
    • (1966) J. Phys. Chem. , vol.70 , pp. 297-300
    • Warren, J.R.1    Gordon, J.A.2
  • 33
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethane-sulfonyl-α-shymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethane-sulfonyl-α-shymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 35
    • 0032571327 scopus 로고    scopus 로고
    • Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins
    • Richieri, G. V., Low, P. J., Ogata, R. T., and Kleinfeld, A. M. (1998) Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins, J. Biol. Chem. 273, 7397-7405.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7397-7405
    • Richieri, G.V.1    Low, P.J.2    Ogata, R.T.3    Kleinfeld, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.