메뉴 건너뛰기




Volumn 286, Issue 4, 1999, Pages 1179-1195

The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure

Author keywords

Cellular retinol binding protein; Lipid transport; Lipid binding protein; NMR; Structure

Indexed keywords

CARBON 13; HELIX LOOP HELIX PROTEIN; NITROGEN 15; RETINOL BINDING PROTEIN;

EID: 0033525633     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2544     Document Type: Article
Times cited : (35)

References (43)
  • 2
    • 0032496377 scopus 로고    scopus 로고
    • Crystal structure of apo-cellular retinoic acid-binding protein type II (R11 M) suggests a mechanism of ligand entry
    • Chen X., Tordova M., Gilliland G. L., Wang L., Li Y., Yan H., Ji X. Crystal structure of apo-cellular retinoic acid-binding protein type II (R11 M) suggests a mechanism of ligand entry. J. Mol. Biol. 278:1998;641-653.
    • (1998) J. Mol. Biol. , vol.278 , pp. 641-653
    • Chen, X.1    Tordova, M.2    Gilliland, G.L.3    Wang, L.4    Li, Y.5    Yan, H.6    Ji, X.7
  • 3
    • 0026354017 scopus 로고
    • Alteration of the binding specificity of cellular retinol-binding protein II by site-directed mutagenesis
    • Cheng L., Qian S.-J., Rothschild C., d'Avignon A., Lefkowith J. B., Gordon J. I., Li E. Alteration of the binding specificity of cellular retinol-binding protein II by site-directed mutagenesis. J. Biol. Chem. 266:1991;24404-24412.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24404-24412
    • Cheng, L.1    Qian, S.-J.2    Rothschild, C.3    D'Avignon, A.4    Lefkowith, J.B.5    Gordon, J.I.6    Li, E.7
  • 4
    • 0029953212 scopus 로고    scopus 로고
    • Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein
    • Cistola D. P., Kim K., Rogl H., Frieden C. Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein. Biochemistry. 35:1996;7559-7565.
    • (1996) Biochemistry , vol.35 , pp. 7559-7565
    • Cistola, D.P.1    Kim, K.2    Rogl, H.3    Frieden, C.4
  • 5
    • 0025046144 scopus 로고
    • Deviations form the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • Clore G. M., Szabo A., Bax A., Kay L. E., Driscoll P. C., Gronenborn A. M. Deviations form the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112:1990;4989-4991.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 7
    • 0026749335 scopus 로고
    • Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins
    • Herr F. M., Ong D. E. Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins. Biochemistry. 31:1992;6748-6755.
    • (1992) Biochemistry , vol.31 , pp. 6748-6755
    • Herr, F.M.1    Ong, D.E.2
  • 8
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the NMR structure of apo intestinal fatty acid-binding protein in solution: Implications for the mechanism of ligand entry
    • Hodsdon M. E., Cistola D. P. Discrete backbone disorder in the NMR structure of apo intestinal fatty acid-binding protein in solution: implications for the mechanism of ligand entry. Biochemistry. 36:1997a;1450-1460.
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 10
    • 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. 6:1995;198-210.
    • (1995) J. Biomol. NMR , vol.6 , pp. 198-210
    • Hodsdon, M.E.1    Toner, J.J.2    Cistola, D.P.3
  • 11
    • 0030573021 scopus 로고    scopus 로고
    • The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm
    • Hodsdon M. E., Ponder J. W., Cistola D. P. The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm. J. Mol. Biol. 264:1996;585-602.
    • (1996) J. Mol. Biol. , vol.264 , pp. 585-602
    • Hodsdon, M.E.1    Ponder, J.W.2    Cistola, D.P.3
  • 12
    • 0027536858 scopus 로고
    • Ligand-protein electrostatic interactions govern the specificity of retinol- And fatty acid-binding proteins
    • Jakoby M. G., I V., Miller K. R., Toner J. J., Bauman A., Cheng L., Li E., Cistola D. P. Ligand-protein electrostatic interactions govern the specificity of retinol- and fatty acid-binding proteins. Biochemistry. 32:1993;872-878.
    • (1993) Biochemistry , vol.32 , pp. 872-878
    • Jakoby, M.G.1    I., V.2    Miller, K.R.3    Toner, J.J.4    Bauman, A.5    Cheng, L.6    Li, E.7    Cistola, D.P.8
  • 13
    • 0028279843 scopus 로고
    • Cellular retinoid-binding proteins: Limited proteolysis reveals a conformational change upon ligand binding
    • Jamison R. S., Newcomer M. E., Ong D. E. Cellular retinoid-binding proteins: limited proteolysis reveals a conformational change upon ligand binding. Biochemistry. 33:1994;2873-2879.
    • (1994) Biochemistry , vol.33 , pp. 2873-2879
    • Jamison, R.S.1    Newcomer, M.E.2    Ong, D.E.3
  • 14
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 15
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 16
    • 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. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;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
  • 17
    • 0029032451 scopus 로고
    • Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy
    • Lassen D., Lücke C., Kveder M., Mesgarzadeh A., Schmidt J. M., Specht B., Lezius A., Spener F., Rüterjans H. Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy. Eur. J. Biochem. 230:1995;266-280.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 266-280
    • Lassen, D.1    Lücke, C.2    Kveder, M.3    Mesgarzadeh, A.4    Schmidt, J.M.5    Specht, B.6    Lezius, A.7    Spener, F.8    Rüterjans, H.9
  • 18
    • 0029846699 scopus 로고    scopus 로고
    • Structure/function of cytoplasmic vitamin A-binding proteins
    • Li E., Norris A. W. Structure/function of cytoplasmic vitamin A-binding proteins. Annu. Rev. Nutr. 16:1996;205-234.
    • (1996) Annu. Rev. Nutr. , vol.16 , pp. 205-234
    • Li, E.1    Norris, A.W.2
  • 19
    • 0023645595 scopus 로고
    • Characterization of rat cellular retinol-binding protein II expressed in Escherichia coli
    • Li E., Locke B., Yang N.-C. C., Ong D. E., Gordon J. I. Characterization of rat cellular retinol-binding protein II expressed in Escherichia coli. J. Biol. Chem. 262:1987;13773-13779.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13773-13779
    • Li, E.1    Locke, B.2    Yang, N.-C.C.3    Ong, D.E.4    Gordon, J.I.5
  • 20
    • 0024412948 scopus 로고
    • Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol-binding protein II produced inEscherichia coli
    • Li E., Qian S.-J., Nader L., Yang N.-C. C., d'Avignon A., Sacchettini J. C., Gordon J. I. Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol-binding protein II produced inEscherichia coli. J. Biol. Chem. 264:1989;17041-17048.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17041-17048
    • Li, E.1    Qian, S.-J.2    Nader, L.3    Yang, N.-C.C.4    D'Avignon, A.5    Sacchettini, J.C.6    Gordon, J.I.7
  • 21
    • 0025907475 scopus 로고
    • Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli
    • Li E., Qian S.-J., Winter N. S., d'Avignon A., Levin M. S., Gordon J. I. Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli. J. Biol. Chem. 266:1991;3622-3629.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3622-3629
    • Li, E.1    Qian, S.-J.2    Winter, N.S.3    D'Avignon, A.4    Levin, M.S.5    Gordon, J.I.6
  • 22
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. Theory and range of validity
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. Theory and range of validity. J. Am. Chem. Soc. 104:1982;4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 23
    • 0030586026 scopus 로고    scopus 로고
    • Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein
    • Lücke C., Zhang F., Rüterjans H., Hamilton J. A., Sacchettini J. C. Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Structure. 4:1996;785-800.
    • (1996) Structure , vol.4 , pp. 785-800
    • Lücke, C.1    Zhang, F.2    Rüterjans, H.3    Hamilton, J.A.4    Sacchettini, J.C.5
  • 24
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram D. R., Kay L. E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. ser. B. 103:1994;203-216.
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 25
    • 0003035905 scopus 로고
    • Cellular retinoid binding proteins
    • M. B. Sporn, A. B. Robert, & D. S. Goodman. New York: Raven Press Ltd
    • Ong D. E., Newcomer M. E., Chytil F. Cellular retinoid binding proteins. Sporn M. B., Robert A. B., Goodman D. S. The Retinoids: Biology, Chemistry, and Medicine. 1994;283-312 Raven Press Ltd, New York.
    • (1994) The Retinoids: Biology, Chemistry, and Medicine , pp. 283-312
    • Ong, D.E.1    Newcomer, M.E.2    Chytil, F.3
  • 26
    • 0030942576 scopus 로고    scopus 로고
    • Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein
    • Ory J., Kane C. D., Simpson M. A., Banaszak L. J., Bernlohr D. A. Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein. J. Biol. Chem. 272:1997;9793-9801.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9793-9801
    • Ory, J.1    Kane, C.D.2    Simpson, M.A.3    Banaszak, L.J.4    Bernlohr, D.A.5
  • 27
    • 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., Kleinfeld A. M. Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins. J. Biol. Chem. 273:1998;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
  • 28
    • 0028170330 scopus 로고
    • NMR studies of fluororetinol analogs complexed to two homologous cellular retinol-binding proteins
    • Rong D., Lovey A. J., Rosenberger M., d'Avignon A., Li E. NMR studies of fluororetinol analogs complexed to two homologous cellular retinol-binding proteins. Biochem. Biophys. Acta. 1208:1994;136-144.
    • (1994) Biochem. Biophys. Acta , vol.1208 , pp. 136-144
    • Rong, D.1    Lovey, A.J.2    Rosenberger, M.3    D'Avignon, A.4    Li, E.5
  • 29
    • 0024356436 scopus 로고
    • The crystal structure of rat intestinal fatty acid binding protein: Refinement and analysis of theE. coli -derived protein with bound palmitate
    • Sacchettini J. C., Gordon J. I., Banaszak L. J. The crystal structure of rat intestinal fatty acid binding protein: refinement and analysis of theE. coli -derived protein with bound palmitate. J. Mol. Biol. 208:1989;327-340.
    • (1989) J. Mol. Biol. , vol.208 , pp. 327-340
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 30
    • 0026712235 scopus 로고
    • Refinement of the structure of recombinant rat intestinal fatty-acid binding apoprotein at 1.2 Å resolution
    • Scapin G., Gordon J. I., Sacchettini J. C. Refinement of the structure of recombinant rat intestinal fatty-acid binding apoprotein at 1.2 Å resolution. J. Biol. Chem. 267:1992;4253-4269.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4253-4269
    • Scapin, G.1    Gordon, J.I.2    Sacchettini, J.C.3
  • 31
    • 0032483133 scopus 로고    scopus 로고
    • Analysis of a series of phenylalanine 57 mutants of the adipocyte lipid-binding protein
    • Simpson M. A., Bernlohr D. A. Analysis of a series of phenylalanine 57 mutants of the adipocyte lipid-binding protein. Biochemistry. 37:1998;10980-10986.
    • (1998) Biochemistry , vol.37 , pp. 10980-10986
    • Simpson, M.A.1    Bernlohr, D.A.2
  • 32
    • 0031776786 scopus 로고    scopus 로고
    • The three- dimensional structure of a helix-less variant of intestinal fatty acid-binding protein
    • Steele R. A., Emmert D. A., Kao J., Hodsdon M. E., Frieden C., Cistola D. P. The three- dimensional structure of a helix-less variant of intestinal fatty acid-binding protein. Protein Sci. 7:1998;1332-1339.
    • (1998) Protein Sci. , vol.7 , pp. 1332-1339
    • Steele, R.A.1    Emmert, D.A.2    Kao, J.3    Hodsdon, M.E.4    Frieden, C.5    Cistola, D.P.6
  • 33
    • 0029125852 scopus 로고
    • Crystal structure of cellular retinoic acid binding protein I show increased access to the binding cavity due to formation of an intermolecular β-sheet
    • Thompson J. R., Bratt J. M., Banaszak L. J. Crystal structure of cellular retinoic acid binding protein I show increased access to the binding cavity due to formation of an intermolecular β-sheet. J. Mol. Biol. 252:1995;433-446.
    • (1995) J. Mol. Biol. , vol.252 , pp. 433-446
    • Thompson, J.R.1    Bratt, J.M.2    Banaszak, L.J.3
  • 34
    • 0029586726 scopus 로고
    • Essential dynamics of the cellular retinol-binding protein - evidence for ligand-induced conformational changes
    • Van Aalten D. M. F., Findlay J. B. C., Amadei A., Berendsen H. J. C. Essential dynamics of the cellular retinol-binding protein - evidence for ligand-induced conformational changes. Protein Eng. 8:1995;1129-1135.
    • (1995) Protein Eng. , vol.8 , pp. 1129-1135
    • Van Aalten, D.M.F.1    Findlay, J.B.C.2    Amadei, A.3    Berendsen, H.J.C.4
  • 35
    • 0031019423 scopus 로고    scopus 로고
    • Engineering protein mechanics: Inhibition of concerted motions of the cellular retinol binding protein by site-directed mutagenesis
    • Van Aalten D. M. F., Jones P. C., De Sousa M., Findlay J. B. C. Engineering protein mechanics: inhibition of concerted motions of the cellular retinol binding protein by site-directed mutagenesis. Protein Eng. 10:1997;31-37.
    • (1997) Protein Eng. , vol.10 , pp. 31-37
    • Van Aalten, D.M.F.1    Jones, P.C.2    De Sousa, M.3    Findlay, J.B.C.4
  • 36
    • 0031036744 scopus 로고    scopus 로고
    • Structure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants
    • Wang L., Li Y., Yan H. Structure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants. J. Biol. Chem. 272:1997;1541-1547.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1541-1547
    • Wang, L.1    Li, Y.2    Yan, H.3
  • 37
    • 0032530468 scopus 로고    scopus 로고
    • NMR solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding
    • Wang L., Li Y., Abildgaard F., Markley J. L., Yan H. NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Biochemistry. 37:1998;12727-12736.
    • (1998) Biochemistry , vol.37 , pp. 12727-12736
    • Wang, L.1    Li, Y.2    Abildgaard, F.3    Markley, J.L.4    Yan, H.5
  • 38
    • 0027213028 scopus 로고
    • Crystal structures of holo and apo-cellular retinol-binding protein II
    • Winter N. S., Bratt J. M., Banaszak L. J. Crystal structures of holo and apo-cellular retinol-binding protein II. J. Mol. Biol. 230:1993;1247-1259.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1247-1259
    • Winter, N.S.1    Bratt, J.M.2    Banaszak, L.J.3
  • 41
    • 0027480327 scopus 로고
    • The adipocyte lipid-binding protein at 1.6-Å resolution: Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids
    • Xu Z., Bernlohr D. A., Banaszak L. J. The adipocyte lipid-binding protein at 1.6-Å resolution: crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids. J. Biol. Chem. 268:1993;7874-7884.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7874-7884
    • Xu, Z.1    Bernlohr, D.A.2    Banaszak, L.J.3
  • 42
    • 0031113230 scopus 로고    scopus 로고
    • Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit
    • Zhang F., Lücke C., Baier L. J., Sacchettini J. C., Hamilton J. A. Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit. J. Biomol. NMR. 9:1997;213-228.
    • (1997) J. Biomol. NMR , vol.9 , pp. 213-228
    • Zhang, F.1    Lücke, C.2    Baier, L.J.3    Sacchettini, J.C.4    Hamilton, J.A.5
  • 43
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR. 4:1994;845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.