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Volumn 50, Issue 2, 2003, Pages 312-328

Insights into the bile acid transportation system: The human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures

Author keywords

Bile acid binding; Ileal transport; Lipid binding protein; NMR spectroscopy; Protein ligand interaction

Indexed keywords

BILE ACID; CARRIER PROTEIN; ILEAL LIPID BINDING PROTEIN; ILEAL LIPID BINDING PROTEIN CHOLYLTAURINE COMPLEX; UNCLASSIFIED DRUG;

EID: 0037297401     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10289     Document Type: Article
Times cited : (50)

References (93)
  • 3
    • 0023792885 scopus 로고
    • The complete amino acid sequence of porcine gastrotropin, an ileal protein which stimulates gastric acid and pepsinogen secretion
    • Walz DA, Wider MD, Snow JW, Dass C, Desiderio DM The complete amino acid sequence of porcine gastrotropin, an ileal protein which stimulates gastric acid and pepsinogen secretion J Biol Chem 1988;263:14189-14195.
    • (1988) J Biol Chem , vol.263 , pp. 14189-14195
    • Walz, D.A.1    Wider, M.D.2    Snow, J.W.3    Dass, C.4    Desiderio, D.M.5
  • 4
    • 0025140903 scopus 로고
    • Identification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes
    • (a) Lin MC, Kramer W, Wilson FA. Identification of cytosolic and microsomal bile acid-binding proteins in rat ileal enterocytes. J Biol Chem 1990;265:14986-14995.
    • (1990) J Biol Chem , vol.265 , pp. 14986-14995
    • Lin, M.C.1    Kramer, W.2    Wilson, F.A.3
  • 5
    • 0028307276 scopus 로고
    • Molecular cloning, tissue distribution, and expression of a 14-kDa bile acid-binding protein from rat ileal cytosol
    • (b) Gong YZ, Everett ET, Schwarz DA, Norris JS, Wilson FA. Molecular cloning, tissue distribution, and expression of a 14-kDa bile acid-binding protein from rat ileal cytosol. Proc Natl Acad Sci USA 1994;91:4741-4745.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4741-4745
    • Gong, Y.Z.1    Everett, E.T.2    Schwarz, D.A.3    Norris, J.S.4    Wilson, F.A.5
  • 6
    • 0029075432 scopus 로고
    • Cloning and chromosomal localization of the human ileal lipid-binding protein
    • (c) Oelkers P, Dawson PA. Cloning and chromosomal localization of the human ileal lipid-binding protein. Biochim Biophys Acta 1995;1257:199-202.
    • (1995) Biochim Biophys Acta , vol.1257 , pp. 199-202
    • Oelkers, P.1    Dawson, P.A.2
  • 7
    • 0021126592 scopus 로고
    • Isolation and partial characterization of an entero-oxyntin from porcine ileum
    • (d) Wider MD, Vinik AI, Heldsinger A. Isolation and partial characterization of an entero-oxyntin from porcine ileum. Endocrinology 1984;115:1484-1491.
    • (1984) Endocrinology , vol.115 , pp. 1484-1491
    • Wider, M.D.1    Vinik, A.I.2    Heldsinger, A.3
  • 8
    • 0024377257 scopus 로고
    • Gastrotropin: Not an enterooxyntin but a member of a family of cytoplasmic hydrophobic ligand binding proteins
    • (e) Gantz I, Nothwehr SF, Del Valle J, Banaszak LJ, Naud M, Gordon JI, Yamada T. Gastrotropin: Not an enterooxyntin but a member of a family of cytoplasmic hydrophobic ligand binding proteins. J Biol Chem 1989;264:20248-20254.
    • (1989) J Biol Chem , vol.264 , pp. 20248-20254
    • Gantz, I.1    Nothwehr, S.F.2    Del Valle, J.3    Banaszak, L.J.4    Naud, M.5    Gordon, J.I.6    Yamada, T.7
  • 9
    • 0025894881 scopus 로고
    • Characterization of a novel 14 kDa bile acid-binding protein from rat ileal cytosol
    • (f) Lin MC, Gong Y, Geoghegan KF, Wilson FA. Characterization of a novel 14 kDa bile acid-binding protein from rat ileal cytosol. Biochim Biophys Acta 1991;1078:329-336.
    • (1991) Biochim Biophys Acta , vol.1078 , pp. 329-336
    • Lin, M.C.1    Gong, Y.2    Geoghegan, K.F.3    Wilson, F.A.4
  • 11
    • 0028101023 scopus 로고
    • The mouse ileal lipid-binding protein gene: A model for studying axial patterning during gut morphogenesis
    • (h) Crossmann MW, Hauft SM, Gordon JI. The mouse ileal lipid-binding protein gene: A model for studying axial patterning during gut morphogenesis. J Cell Biol 1994;126:1547-1564.
    • (1994) J Cell Biol , vol.126 , pp. 1547-1564
    • Crossmann, M.W.1    Hauft, S.M.2    Gordon, J.I.3
  • 13
    • 0012360083 scopus 로고    scopus 로고
    • Properties and specificity of the rabbit ileal Na+/bile acid co-transport system
    • Paumgartner G, Gerok W, Stiehl A, editors. Dordrecht, Netherlands: Kluwer Academic Publishers Group
    • Kramer W, Stengelin S, Wess G. Properties and specificity of the rabbit ileal Na+/bile acid co-transport system. In: Paumgartner G, Gerok W, Stiehl A, editors. Bile Acids in Hepatobiliary Diseases: Basic Research and Clinical Application. Dordrecht, Netherlands: Kluwer Academic Publishers Group; 1997. p 161-178.
    • (1997) Bile Acids in Hepatobiliary Diseases: Basic Research and Clinical Application , pp. 161-178
    • Kramer, W.1    Stengelin, S.2    Wess, G.3
  • 15
    • 0027250469 scopus 로고
    • Sodium-dependent bile acid transport activity in rabbit small intestine correlates with the coexpression of an integral 93-kDa and a peripheral 14-kDa bile acid-binding membrane protein along the duodenum-ileum axis
    • (b) Kramer W, Girbig F, Gutjahr U, Kowalewski S, Jouvenal K, Müller G, Tripier D, Wess G. Sodium-dependent bile acid transport activity in rabbit small intestine correlates with the coexpression of an integral 93-kDa and a peripheral 14-kDa bile acid-binding membrane protein along the duodenum-ileum axis. J Biol Chem 1993;268:18035-18046.
    • (1993) J Biol Chem , vol.268 , pp. 18035-18046
    • Kramer, W.1    Girbig, F.2    Gutjahr, U.3    Kowalewski, S.4    Jouvenal, K.5    Müller, G.6    Tripier, D.7    Wess, G.8
  • 16
    • 0028890296 scopus 로고
    • Radiation-inactivation analysis of the Na+/bile acid co-transport system from rabbit ileum
    • (c) Kramer W, Girbig F, Gutjahr U, Kowalewski S. Radiation-inactivation analysis of the Na+/bile acid co-transport system from rabbit ileum. Biochem J 1995;305:241-246.
    • (1995) Biochem J , vol.305 , pp. 241-246
    • Kramer, W.1    Girbig, F.2    Gutjahr, U.3    Kowalewski, S.4
  • 17
    • 0026098687 scopus 로고
    • Structural and functional features of different types of cytoplasmic fatty acid-binding proteins
    • (a) Veerkamp JH, Peeters RA, Maatman RGHJ. Structural and functional features of different types of cytoplasmic fatty acid-binding proteins. Biochim Biophys Acta 1991;1081:1-24.
    • (1991) Biochim Biophys Acta , vol.1081 , pp. 1-24
    • Veerkamp, J.H.1    Peeters, R.A.2    Maatman, R.G.H.J.3
  • 18
    • 0028896925 scopus 로고
    • Cytoplasmic fatty acid-binding proteins: Their structure and genes
    • (b) Veerkamp JH, Maatman RGHJ. Cytoplasmic fatty acid-binding proteins: Their structure and genes. Prog Lipid Res 1995;34:17-52.
    • (1995) Prog Lipid Res , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.G.H.J.2
  • 20
    • 0023874788 scopus 로고
    • The structure of crystalline Escherischia coli-derived rat intestinal fatty acid-binding protein at 2.5 Å resolution
    • (a) Sacchettini JC, Gordon JI, Banaszak LJ. The structure of crystalline Escherischia coli-derived rat intestinal fatty acid-binding protein at 2.5 Å resolution. J Biol Chem 1988;263:5815-5819.
    • (1988) J Biol Chem , vol.263 , pp. 5815-5819
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 21
    • 0024359144 scopus 로고
    • Refined apoprotein structure of rat intestinal fatty acid-binding protein produced in Escherischia coli
    • (b) Sacchettini JC, Gordon JI, Banaszak LJ. Refined apoprotein structure of rat intestinal fatty acid-binding protein produced in Escherischia coli. Proc Natl Acad Sci USA 1989;86:7736 -7740.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7736-7740
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 22
    • 0026712235 scopus 로고
    • Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution
    • (c) Scapin G, Gordon JI, Sacchettini JC. Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution. J Biol Chem 1992;267:4253-4269.
    • (1992) J Biol Chem , vol.267 , pp. 4253-4269
    • Scapin, G.1    Gordon, J.I.2    Sacchettini, J.C.3
  • 23
    • 0025003049 scopus 로고
    • Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 Å resolution
    • (a) Scapin G, Spadon P, Mammi M, Zanotti G, Monaco HL. Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 Å resolution. Mol Cell Biochem 1990;98:95-99.
    • (1990) Mol Cell Biochem , vol.98 , pp. 95-99
    • Scapin, G.1    Spadon, P.2    Mammi, M.3    Zanotti, G.4    Monaco, H.L.5
  • 24
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • (b) Thompson J, Winter N, Terwey D, Bratt J, Banaszak L. The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates. J Biol Chem 1997;272:7140-7150.
    • (1997) J Biol Chem , vol.272 , pp. 7140-7150
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4    Banaszak, L.5
  • 26
    • 0026736804 scopus 로고
    • Three-dimensional structure of recombinant human muscle fatty acid-binding protein
    • Zanotti G, Scapin G, Spadon P, Veerkamp JH, Sacchettini JC. Three-dimensional structure of recombinant human muscle fatty acid-binding protein. J Biol Chem 1992;267:18541-18550.
    • (1992) J Biol Chem , vol.267 , pp. 18541-18550
    • Zanotti, G.1    Scapin, G.2    Spadon, P.3    Veerkamp, J.H.4    Sacchettini, J.C.5
  • 27
    • 0026554620 scopus 로고
    • Crystal structure of recombinant murine adipocyte lipid-binding protein
    • Xu Z, Bernlohr DA, Banaszak LJ. Crystal structure of recombinant murine adipocyte lipid-binding protein. Biochemistry 1992;31:3484-3492.
    • (1992) Biochemistry , vol.31 , pp. 3484-3492
    • Xu, Z.1    Bernlohr, D.A.2    Banaszak, L.J.3
  • 28
    • 0024027281 scopus 로고
    • The three-dimensional structure of P2 myelin protein
    • (a) Jones TA, Bergfors T, Sedzik J, Unge T. The three-dimensional structure of P2 myelin protein. EMBO J 1988;7:1597-1604.
    • (1988) EMBO J , vol.7 , pp. 1597-1604
    • Jones, T.A.1    Bergfors, T.2    Sedzik, J.3    Unge, T.4
  • 29
    • 0027310780 scopus 로고
    • Crystallographic studies on a family of cellular lipophilic transport proteins: The refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans retinol
    • (b) Cowan SW, Newcomer ME, Jones TA. Crystallographic studies on a family of cellular lipophilic transport proteins: The refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans retinol. J Mol Biol 1993;230:1225-1246.
    • (1993) J Mol Biol , vol.230 , pp. 1225-1246
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 30
    • 0026486537 scopus 로고
    • Crystallization, structure determination and least-squares refinement to 1.75 Å resolution of the fatty acid binding protein isolated from Manducta sexta L.
    • Benning MM, Smith AF, Wells MA, Holden HM. Crystallization, structure determination and least-squares refinement to 1.75 Å resolution of the fatty acid binding protein isolated from Manducta sexta L. J Mol Biol 1992;228:208-219.
    • (1992) J Mol Biol , vol.228 , pp. 208-219
    • Benning, M.M.1    Smith, A.F.2    Wells, M.A.3    Holden, H.M.4
  • 31
    • 0027213028 scopus 로고
    • Crystal structure of holoand apo-cellular retinol-binding protein II
    • (a) Winter NS, Bratt JM, Banaszak LJ. Crystal structure of holoand apo-cellular retinol-binding protein II. J Mol Biol 1993;230:1247-1259.
    • (1993) J Mol Biol , vol.230 , pp. 1247-1259
    • Winter, N.S.1    Bratt, J.M.2    Banaszak, L.J.3
  • 32
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • (b) Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, Jones TA. Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 1994;2:1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 33
    • 0030586026 scopus 로고    scopus 로고
    • Flexibility is a likely determinant of binding in the case of ileal lipid-binding protein
    • Lücke C, Zhang F, Rüterjans H, Hamilton JA, Sacchettini JC. Flexibility is a likely determinant of binding in the case of ileal lipid-binding protein. Structure 1996;4:785-800.
    • (1996) Structure , vol.4 , pp. 785-800
    • Lücke, C.1    Zhang, F.2    Rüterjans, H.3    Hamilton, J.A.4    Sacchettini, J.C.5
  • 35
    • 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 JM, Specht B, Lezius A, Spener F, Rtiterjans H. Three-dimensional structure of bovine heart fatty acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy. Eur J Biochem 1995;230:266-280.
    • (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    Rtiterjans, H.9
  • 36
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry
    • (a) Hodsdon ME, Cistola DP. Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: implications for the mechanism of ligand entry. Biochemistry 1997;36:1450-1460.
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 37
    • 0031113230 scopus 로고    scopus 로고
    • Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit
    • (b) Zhang F, Lücke C, Baier LJ, Sacchettini JC, Hamilton JA. Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit. J Biomol NMR 1997;9:213-228.
    • (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
  • 38
    • 0032530468 scopus 로고    scopus 로고
    • NMR solution structure of type II human cellular retinoic acid binding protein: Implications for lipid binding
    • Wang L, Li Y, Abildgaard F, Markley JL, Yan H. NMR solution structure of type II human cellular retinoic acid binding protein: Implications for lipid binding. Biochemistry 1998;37:12727-12736.
    • (1998) Biochemistry , vol.37 , pp. 12727-12736
    • Wang, L.1    Li, Y.2    Abildgaard, F.3    Markley, J.L.4    Yan, H.5
  • 39
    • 0033525633 scopus 로고    scopus 로고
    • He structure and dynamics of rat apo cellular retinol-bindimng protein II in solution: Comparison with the x-ray structure
    • Lu J, Lin CL, Tang C, Ponder JW, Kao JLF, Cistola DP, Li E. He structure and dynamics of rat apo cellular retinol-bindimng protein II in solution: Comparison with the x-ray structure. J Mol Biol 1999;286:1179-1195.
    • (1999) J Mol Biol , vol.286 , pp. 1179-1195
    • Lu, J.1    Lin, C.L.2    Tang, C.3    Ponder, J.W.4    Kao, J.L.F.5    Cistola, D.P.6    Li, E.7
  • 40
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540. (http://scop.mrc-lmb.cam.ac.uk/scop)
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 41
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin C, Bohacek RS. QXP: Powerful, rapid computer algorithms for structure-based drug design. J Comput Aided Mol Des 1997;113:33-344.
    • (1997) J Comput Aided Mol Des , vol.113 , pp. 33-344
    • McMartin, C.1    Bohacek, R.S.2
  • 42
    • 0000067620 scopus 로고    scopus 로고
    • Combining structure-based design and 3D-QSAR towards the discovery of non-chiral, potent and selective factor Xa inhibitors
    • Höltje H-D, Sippl W, editors. Barcelona: Prous Science
    • Matter H, Defossa E, Heinelt U, Naumann T, Schreuder H, Wildgoose P. Combining structure-based design and 3D-QSAR towards the discovery of non-chiral, potent and selective factor Xa inhibitors. In: Höltje H-D, Sippl W, editors. Rational Approaches in Drug Design. Barcelona: Prous Science; 2001. p 177-185.
    • (2001) Rational Approaches in Drug Design , pp. 177-185
    • Matter, H.1    Defossa, E.2    Heinelt, U.3    Naumann, T.4    Schreuder, H.5    Wildgoose, P.6
  • 43
    • 0037030707 scopus 로고    scopus 로고
    • Structural classification of protein kinases using 3D molecular interaction field analysis of their ligand binding sites: Target family landscapes
    • Naumann T, Matter H. Structural classification of protein kinases using 3D molecular interaction field analysis of their ligand binding sites: Target family landscapes. J Med Chem 2002;45:2366-2378.
    • (2002) J Med Chem , vol.45 , pp. 2366-2378
    • Naumann, T.1    Matter, H.2
  • 46
    • 0012399691 scopus 로고    scopus 로고
    • Bruker Analytische Messtechnik GmbH
    • Bruker XWINNMR Software Manual. Bruker Analytische Messtechnik GmbH, 2000.
    • (2000) Bruker XWINNMR Software Manual
  • 48
    • 0012433038 scopus 로고    scopus 로고
    • St. Louis, MO: Tripos
    • SYBYL TRIAD, Version 6.7, St. Louis, MO: Tripos, 2001.
    • (2001) SYBYL TRIAD Version 6.7
  • 49
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier BH, Bachmann P, Ernst RR. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 1979;71:4546-4553.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 51
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 1985;65:355-360.
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 52
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins
    • Marion D, Wüthrich K. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins. Biochem Biophys Res Commun 1983;113:967-974.
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 53
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G, Ruben DJ. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 1980;69:185-189.
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 55
    • 0024595889 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a
    • (b) Zuiderweg ERP, Fesik SW. Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry 1989;28:2387-2391.
    • (1989) Biochemistry , vol.28 , pp. 2387-2391
    • Zuiderweg, E.R.P.1    Fesik, S.W.2
  • 56
    • 0025210153 scopus 로고
    • Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy
    • Driscoll PC, Clore GM, Marion D, Wingfield PT, Gronenborn AM. Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy. Biochemistry 1990;29:3542-3556.
    • (1990) Biochemistry , vol.29 , pp. 3542-3556
    • Driscoll, P.C.1    Clore, G.M.2    Marion, D.3    Wingfield, P.T.4    Gronenborn, A.M.5
  • 57
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay LE, Ikura M, Tschudin R, Bax A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J Magn Reson 1990;89:496-514.
    • (1990) J Magn Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 59
    • 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
    • (a) Güntert P, Braun W, Wüthrich K. 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 1991;217:517-530.
    • (1991) J Mol Biol , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 60
    • 0026011496 scopus 로고
    • Structure determination of the Antp(C39 → S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA
    • (b) Güntert P, Qian YQ, Otting G, Müller M, Gehring W, Wüthrich K. Structure determination of the Antp(C39 → S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA. J Mol Biol 1991;217:531-540.
    • (1991) J Mol Biol , vol.217 , pp. 531-540
    • Güntert, P.1    Qian, Y.Q.2    Otting, G.3    Müller, M.4    Gehring, W.5    Wüthrich, K.6
  • 62
    • 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. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J Biomol NMR 1991;1:447-456.
    • (1991) J Biomol NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 63
    • 84988115618 scopus 로고
    • Validation of the general purpose tripos 5.2 force field
    • Clark M, Cramer III RD, Van Opdenbosch N. Validation of the general purpose tripos 5.2 force field. J Comp Chem 1989;10:982-1012.
    • (1989) J Comp Chem , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer, R.D.2    Van Opdenbosch, N.3
  • 64
    • 2142813682 scopus 로고
    • Molecular dynamics computer simulation. Method, application and perspectives in chemistry
    • van Gunsteren WF, Berendsen HJC. Molecular dynamics computer simulation. Method, application and perspectives in chemistry. Angew Chem Int Ed Engl 1990;29:992-1023.
    • (1990) Angew Chem Int Ed Engl , vol.29 , pp. 992-1023
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 65
    • 84913537730 scopus 로고
    • Fast generation of molecular surfaces from 3D data fields with enhanced marching cube algorithm
    • (a) Heiden W, Goetze T, Brickmann J. Fast generation of molecular surfaces from 3D data fields with enhanced marching cube algorithm. J Comp Chem 1993;14:246-250.
    • (1993) J Comp Chem , vol.14 , pp. 246-250
    • Heiden, W.1    Goetze, T.2    Brickmann, J.3
  • 67
    • 85006889147 scopus 로고    scopus 로고
    • Implemented in SYBYL 6.5. St. Louis, MO: Tripos, 1999
    • (c) Implemented in SYBYL 6.5. St. Louis, MO: Tripos, 1999.
  • 68
    • 0027673371 scopus 로고
    • A new approach to the display of local lipophilicity/hydrophilicity mapped on molecular surfaces
    • Heiden W, Moeckel G, Brickmann J. A new approach to the display of local lipophilicity/hydrophilicity mapped on molecular surfaces. J Comp Aided Mol Design 1993;7:503-514.
    • (1993) J Comp Aided Mol Design , vol.7 , pp. 503-514
    • Heiden, W.1    Moeckel, G.2    Brickmann, J.3
  • 69
    • 84988109729 scopus 로고
    • Atomic physicochemical parameters for three-dimensional structure-directed quantitative structure-activity relationships. 1. Partition coefficients as a measure of hydrophobicity
    • (a) Ghose A, Crippen G. Atomic physicochemical parameters for three-dimensional structure-directed quantitative structure-activity relationships. 1. Partition coefficients as a measure of hydrophobicity. J Comp Chem 1986;7:565-577.
    • (1986) J Comp Chem , vol.7 , pp. 565-577
    • Ghose, A.1    Crippen, G.2
  • 70
    • 0024716284 scopus 로고
    • Atomic physicochemical parameters for three-dimensional structure-directed quantitative structure-activity relationships. 4. Additional parameters for hydrophobic and dispersive interactions and their application for an automated superposition of certain naturally occurring nucleoside antibiotics
    • (b) Viswanadhan VN, Ghose AK, Revankar GR, Robins RK. Atomic physicochemical parameters for three-dimensional structure-directed quantitative structure-activity relationships. 4. Additional parameters for hydrophobic and dispersive interactions and their application for an automated superposition of certain naturally occurring nucleoside antibiotics. J Chem Inf Comput Sci 1989;29:163-172.
    • (1989) J Chem Inf Comput Sci , vol.29 , pp. 163-172
    • Viswanadhan, V.N.1    Ghose, A.K.2    Revankar, G.R.3    Robins, R.K.4
  • 71
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • (a) Connolly ML. Solvent-accessible surfaces of proteins and nucleic acids. Science 1983;221:709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 72
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • (b) Connolly ML. Analytical molecular surface calculation. J Appl Crystallogr 1983;6:548-558.
    • (1983) J Appl Crystallogr , vol.6 , pp. 548-558
    • Connolly, M.L.1
  • 74
    • 85006872518 scopus 로고    scopus 로고
    • (a) RCSB Protein Data Bank, from the Research Collaboratory for Structural Bioinformatics, http://www.rcsb.org/pdb/index.html.
  • 76
    • 0021871375 scopus 로고
    • Computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • (a) Goodford PJA. Computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J Med Chem 1985;28:849-857.
    • (1985) J Med Chem , vol.28 , pp. 849-857
    • Goodford, P.J.A.1
  • 77
    • 0024566942 scopus 로고
    • New hydrogen-bond potentials for use in determining energetically favorable binding sites on molecules of known structure
    • (b) Boobbyer DNA, Goodford PJ, McWhinnie PM, Wade RC. New hydrogen-bond potentials for use in determining energetically favorable binding sites on molecules of known structure. J Med Chem 1989;32:1083-1094.
    • (1989) J Med Chem , vol.32 , pp. 1083-1094
    • Boobbyer, D.N.A.1    Goodford, P.J.2    McWhinnie, P.M.3    Wade, R.C.4
  • 78
    • 0027439587 scopus 로고
    • Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 1. Ligand probe groups with the ability to form two hydrogen bonds
    • (c) Wade RC, Clerk KJ, Goodford PJ. Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 1. Ligand probe groups with the ability to form two hydrogen bonds. J Med Chem 1993;36:140-147.
    • (1993) J Med Chem , vol.36 , pp. 140-147
    • Wade, R.C.1    Clerk, K.J.2    Goodford, P.J.3
  • 79
    • 0027510004 scopus 로고
    • Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds
    • (d) Wade RC, Goodford PJ. Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds. J Med Chem 1993;36:148-156.
    • (1993) J Med Chem , vol.36 , pp. 148-156
    • Wade, R.C.1    Goodford, P.J.2
  • 80
    • 0003609445 scopus 로고    scopus 로고
    • Molecular Discovery Ltd. Elms Parade, Oxford, UK: West Way House
    • GRID Version 18, Molecular Discovery Ltd. Elms Parade, Oxford, UK: West Way House, 2000.
    • (2000) GRID Version 18
  • 84
    • 0024154259 scopus 로고
    • Multivariate data analysis and experimental design in biomedical research
    • Ellis GP, West GB, editors. New York: Elsevier
    • (d) Stahle L, Wold S. Multivariate data analysis and experimental design in biomedical research. In: Ellis GP, West GB, editors. Progress in Medicinal Chemistry. New York: Elsevier; 1988. p 292-338.
    • (1988) Progress in Medicinal Chemistry , pp. 292-338
    • Stahle, L.1    Wold, S.2
  • 87
    • 0027310371 scopus 로고
    • Generating optimal linear PLS estimations (GOLPE): An advanced chemometric tool for handling 3D-QSAR problems
    • Baroni M, Costantino G, Cruciani G, Riganelli D, Valigi R, Clementi S. Generating optimal linear PLS estimations (GOLPE): An advanced chemometric tool for handling 3D-QSAR problems. Quant Struc Act Relat 1993;12:9-20.
    • (1993) Quant Struc Act Relat , vol.12 , pp. 9-20
    • Baroni, M.1    Costantino, G.2    Cruciani, G.3    Riganelli, D.4    Valigi, R.5    Clementi, S.6
  • 88
    • 0000736392 scopus 로고    scopus 로고
    • Analysis of multiblock and hierarchical PCA and PLS models
    • Westerhuis JA, Kourti T, Macgregor JF. Analysis of multiblock and hierarchical PCA and PLS models. J Chemom 1998;12:301-321.
    • (1998) J Chemom , vol.12 , pp. 301-321
    • Westerhuis, J.A.1    Kourti, T.2    Macgregor, J.F.3
  • 90
    • 0000194538 scopus 로고
    • The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination
    • Güntert P, Berndt KD, Wiithrich K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination. J Biomol NMR 1993;3:601-606.
    • (1993) J Biomol NMR , vol.3 , pp. 601-606
    • Güntert, P.1    Berndt, K.D.2    Wiithrich, K.3
  • 91
    • 85006884619 scopus 로고    scopus 로고
    • note
    • Please note different sequence numberings for ILBP in Refs. 18 and 24. For consistency with previous NMR publications, we follow Ref. 18.
  • 92
    • 0035831545 scopus 로고    scopus 로고
    • Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure
    • Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C. Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J Biol Chem 2001;276:7291-7301.
    • (2001) J Biol Chem , vol.276 , pp. 7291-7301
    • Kramer, W.1    Sauber, K.2    Baringhaus, K.H.3    Kurz, M.4    Stengelin, S.5    Lange, G.6    Corsiero, D.7    Girbig, F.8    König, W.9    Weyland, C.10
  • 93
    • 0027096161 scopus 로고
    • Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75 resolution
    • Sacchettini JC, Scapin G, Gopaul D, Gordon JI. Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75 resolution. J Biol Chem 1992;267:23534-23545.
    • (1992) J Biol Chem , vol.267 , pp. 23534-23545
    • Sacchettini, J.C.1    Scapin, G.2    Gopaul, D.3    Gordon, J.I.4


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