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Volumn 50, Issue 8, 2011, Pages 1283-1295

A nuclear magnetic resonance-based structural rationale for contrasting stoichiometry and ligand binding site(s) in fatty acid-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

BOUND LIGANDS; CARBOXYLATE GROUPS; COLLISIONAL INTERACTIONS; CYTOSOLIC; ELECTROSTATIC INTERACTIONS; EXTENDED STRUCTURES; FATTY ACID BINDING; FATTY ACID-BINDING PROTEINS; HYDROPHOBIC CHAINS; LIGAND-BINDING SITES; NMR TITRATION; PROTEIN BINDING; PROTEIN CAVITY; PROTEIN FAMILY; PROTEIN SEQUENCES; PROTEIN SURFACE; PROTEIN-LIGAND COMPLEXES; TERTIARY STRUCTURES; U-SHAPED; WILD TYPES;

EID: 79951870969     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101307h     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • Storch, J. and Thumser, A. E. (2000) The fatty acid transport function of fatty acid-binding proteins Biochim. Biophys. Acta 1486, 28-44
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 28
    • Storch, J.1    Thumser, A.E.2
  • 2
    • 50949128339 scopus 로고    scopus 로고
    • The emerging functions and mechanisms of mammalian fatty acid-binding proteins
    • Storch, J. and Córsico, B. (2008) The emerging functions and mechanisms of mammalian fatty acid-binding proteins Annu. Rev. Nutr. 28, 73-95
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 73
    • Storch, J.1    Córsico, B.2
  • 3
    • 0036634367 scopus 로고    scopus 로고
    • New insights into the structure and function of fatty acid-binding proteins
    • Zimmerman, A. W. and Veerkamp, J. H. (2002) New insights into the structure and function of fatty acid-binding proteins Cell. Mol. Life Sci. 59, 1096-1116
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1096
    • Zimmerman, A.W.1    Veerkamp, J.H.2
  • 4
    • 33646891301 scopus 로고    scopus 로고
    • Fatty-acid-binding protein from the flight muscle of Locusta migratoria: Evolutionary variations in fatty acid binding
    • Lucke, C., Qiao, Y., Van Moerkerk, H. T., Veerkamp, J. H., and Hamilton, J. A. (2006) Fatty-acid-binding protein from the flight muscle of Locusta migratoria: Evolutionary variations in fatty acid binding Biochemistry 45, 6296-6305
    • (2006) Biochemistry , vol.45 , pp. 6296
    • Lucke, C.1    Qiao, Y.2    Van Moerkerk, H.T.3    Veerkamp, J.H.4    Hamilton, J.A.5
  • 6
    • 66349121402 scopus 로고    scopus 로고
    • Structural and functional analysis of fatty acid-binding proteins
    • Storch, J. and McDermott, L. (2009) Structural and functional analysis of fatty acid-binding proteins J. Lipid Res. 50 (Suppl.) S126-S131
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL. , pp. 126
    • Storch, J.1    McDermott, L.2
  • 7
    • 77954656481 scopus 로고    scopus 로고
    • Natural ligand binding and transfer from liver fatty acid binding protein (LFABP) to membranes
    • De Gerónimo, E., Hagan, R. M., Wilton, D. C., and Córsico, B. (2010) Natural ligand binding and transfer from liver fatty acid binding protein (LFABP) to membranes Biochim. Biophys. Acta 1801, 1082-1089
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 1082
    • De Gerónimo, E.1    Hagan, R.M.2    Wilton, D.C.3    Córsico, B.4
  • 8
    • 35848954991 scopus 로고    scopus 로고
    • Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein
    • He, Y., Yang, X., Wang, H., Estephan, R., Francis, F., Kodukula, S., Storch, J., and Stark, R. E. (2007) Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein Biochemistry 46, 12543-12556
    • (2007) Biochemistry , vol.46 , pp. 12543
    • He, Y.1    Yang, X.2    Wang, H.3    Estephan, R.4    Francis, F.5    Kodukula, S.6    Storch, J.7    Stark, R.E.8
  • 9
    • 0026012437 scopus 로고
    • Polyene fatty acid interactions with recombinant intestinal and liver fatty acid-binding proteins
    • Nemecz, G., Jefferson, J. R., and Schroeder, F. (1991) Polyene fatty acid interactions with recombinant intestinal and liver fatty acid-binding proteins J. Biol. Chem. 266, 17112-17123
    • (1991) J. Biol. Chem. , vol.266 , pp. 17112
    • Nemecz, G.1    Jefferson, J.R.2    Schroeder, F.3
  • 10
    • 0024595766 scopus 로고
    • Fatty acid interactions with rat intestinal and liver fatty acid-binding proteins expressed in Escherichia coli
    • Cistola, D. P., Sacchettini, J. C., Banaszak, L. J., Walsh, M. T., and Gordon, J. I. (1989) Fatty acid interactions with rat intestinal and liver fatty acid-binding proteins expressed in Escherichia coli J. Biol. Chem. 264, 2700-2710
    • (1989) J. Biol. Chem. , vol.264 , pp. 2700
    • Cistola, D.P.1    Sacchettini, J.C.2    Banaszak, L.J.3    Walsh, M.T.4    Gordon, J.I.5
  • 11
    • 0032906887 scopus 로고    scopus 로고
    • The liver fatty acid binding protein: Comparison of cavity properties of intracellular lipid-binding proteins
    • Thompson, J., Ory, J., Reese-Wagoner, A., and Banaszak, L. (1999) The liver fatty acid binding protein: Comparison of cavity properties of intracellular lipid-binding proteins Mol. Cell. Biochem. 192, 9-16
    • (1999) Mol. Cell. Biochem. , vol.192 , pp. 9
    • Thompson, J.1    Ory, J.2    Reese-Wagoner, A.3    Banaszak, L.4
  • 12
    • 0024356436 scopus 로고
    • Crystal structure of rat intestinal fatty-acid-binding protein: Refinement and analysis of the Escherichia coli -derived protein with bound palmitate
    • Sacchettini, J. C., Gordon, J. I., and Banaszak, L. (1989) Crystal structure of rat intestinal fatty-acid-binding protein: Refinement and analysis of the Escherichia coli -derived protein with bound palmitate J. Mol. Biol. 208, 327-339
    • (1989) J. Mol. Biol. , vol.208 , pp. 327
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.3
  • 13
    • 0029993073 scopus 로고    scopus 로고
    • Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms
    • Hsu, K. T. and Storch, J. (1996) Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms J. Biol. Chem. 271, 13317-13323
    • (1996) J. Biol. Chem. , vol.271 , pp. 13317
    • Hsu, K.T.1    Storch, J.2
  • 14
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • Thompson, J., Winter, N., Terwey, D., Bratt, J., and Banaszak, L. (1997) The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates J. Biol. Chem. 272, 7140-7150
    • (1997) J. Biol. Chem. , vol.272 , pp. 7140
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4    Banaszak, L.5
  • 15
    • 0027257417 scopus 로고
    • Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver
    • Borchers, T. and Spener, F. (1993) Involvement of arginine in the binding of heme and fatty acids to fatty acid-binding protein from bovine liver Mol. Cell. Biochem. 123, 23-27
    • (1993) Mol. Cell. Biochem. , vol.123 , pp. 23
    • Borchers, T.1    Spener, F.2
  • 16
    • 0027958322 scopus 로고
    • Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein
    • Thumser, A. E., Evans, D., Worrall, A. F., and Wilton, D. C. (1994) Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein Biochem. J. 297, 103-107
    • (1994) Biochem. J. , vol.297 , pp. 103
    • Thumser, A.E.1    Evans, D.2    Worrall, A.F.3    Wilton, D.C.4
  • 17
    • 0029869623 scopus 로고    scopus 로고
    • Mutations of recombinant rat liver fatty acid-binding protein at residues 102 and 122 alter its structural integrity and affinity for physiological ligands
    • Thumser, A. E., Voysey, J., and Wilton, D. C. (1996) Mutations of recombinant rat liver fatty acid-binding protein at residues 102 and 122 alter its structural integrity and affinity for physiological ligands Biochem. J. 314, 943-949
    • (1996) Biochem. J. , vol.314 , pp. 943
    • Thumser, A.E.1    Voysey, J.2    Wilton, D.C.3
  • 19
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • Alexov, E. G. and Gunner, M. R. (1997) Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties Biophys. J. 72, 2075-2093
    • (1997) Biophys. J. , vol.72 , pp. 2075
    • Alexov, E.G.1    Gunner, M.R.2
  • 20
    • 0033614791 scopus 로고    scopus 로고
    • - to QB in bacterial photosynthetic reaction centers
    • - to QB in bacterial photosynthetic reaction centers Biochemistry 38, 8253-8270
    • (1999) Biochemistry , vol.38 , pp. 8253
    • Alexov, E.G.1    Gunner, M.R.2
  • 22
    • 0028076831 scopus 로고
    • Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with fluorescent probe ADIFAB
    • Richieri, G. V., Ogata, R. T., and Kleinfeld, A. M. (1994) Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with fluorescent probe ADIFAB J. Biol. Chem. 269, 23918-23930
    • (1994) J. Biol. Chem. , vol.269 , pp. 23918
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 24
    • 33746606458 scopus 로고    scopus 로고
    • Retinol modulates site-specific mobility of apo-cellular retinol-binding protein to promote ligand binding
    • Mittag, T., Franzoni, L., Cavazzini, D., Schaffhausen, B., Rossi, G. L., and Günther, U. (2006) Retinol modulates site-specific mobility of apo-cellular retinol-binding protein to promote ligand binding J. Am. Chem. Soc. 128, 9844-9848
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9844
    • Mittag, T.1    Franzoni, L.2    Cavazzini, D.3    Schaffhausen, B.4    Rossi, G.L.5    Günther, U.6
  • 26
    • 0033514406 scopus 로고    scopus 로고
    • Dynamics of palmitic acid complexed with rat intestinal fatty acid binding protein
    • Zhu, L., Kurian, E., Prendergast, F. G., and Kemple, M. D. (1999) Dynamics of palmitic acid complexed with rat intestinal fatty acid binding protein Biochemistry 38, 1554-1561
    • (1999) Biochemistry , vol.38 , pp. 1554
    • Zhu, L.1    Kurian, E.2    Prendergast, F.G.3    Kemple, M.D.4
  • 27
    • 0141683523 scopus 로고    scopus 로고
    • NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol
    • Dehner, A., Furrer, J., Richter, K., Schuster, I., Buchner, J., and Kessler, H. (2003) NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol ChemBioChem 4, 870-877
    • (2003) ChemBioChem , vol.4 , pp. 870
    • Dehner, A.1    Furrer, J.2    Richter, K.3    Schuster, I.4    Buchner, J.5    Kessler, H.6
  • 28
    • 0034016522 scopus 로고    scopus 로고
    • NMR study of the differential contributions of residues of transforming growth factor β to association with its receptor
    • McInnes, C., Grothe, S., OConnor-McCourt, M., and Sykes, B. (2000) NMR study of the differential contributions of residues of transforming growth factor β to association with its receptor Protein Eng. 13, 143-147
    • (2000) Protein Eng. , vol.13 , pp. 143
    • McInnes, C.1    Grothe, S.2    Oconnor-Mccourt, M.3    Sykes, B.4
  • 30
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., and Fesik, S. W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR Science 274, 1531-1534
    • (1996) Science , vol.274 , pp. 1531
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 31
    • 1542475806 scopus 로고    scopus 로고
    • NMR-based methods and strategies for drug discovery
    • Salvatella, X. and Giralt, E. (2003) NMR-based methods and strategies for drug discovery Chem. Soc. Rev. 32, 365-372
    • (2003) Chem. Soc. Rev. , vol.32 , pp. 365
    • Salvatella, X.1    Giralt, E.2
  • 32
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • Mulder, F. A. A., Schipper, D., Bott, R., and Boelens, R. (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins J. Mol. Biol. 292, 111-123
    • (1999) J. Mol. Biol. , vol.292 , pp. 111
    • Mulder, F.A.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 33
    • 0034673316 scopus 로고    scopus 로고
    • The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands
    • Medek, A., Hajduk, P. J., Mack, J., and Fesik, S. W. (2000) The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands J. Am. Chem. Soc. 122, 1241-1242
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1241
    • Medek, A.1    Hajduk, P.J.2    MacK, J.3    Fesik, S.W.4
  • 34
    • 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
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 36
  • 37
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Blevins, R. A. (1994) NMR View: A computer program for the visualization and analysis of NMR data J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603
    • Johnson, B.A.1    Blevins, R.A.2
  • 39
    • 1542345719 scopus 로고    scopus 로고
    • Fatty acid interactions with proteins: What X-ray crystal and NMR solution structures tell us
    • DOI 10.1016/j.plipres.2003.09.002, PII S0163782703000523
    • Hamilton, J. (2004) Fatty acid interactions with proteins: What X-ray crystal and NMR solution structures tell us Prog. Lipid Res. 43, 177-199 (Pubitemid 38299192)
    • (2004) Progress in Lipid Research , vol.43 , Issue.3 , pp. 177-199
    • Hamilton, J.A.1
  • 40
    • 0032701131 scopus 로고    scopus 로고
    • Liver fatty acid binding protein: Species variation and the accommodation of different ligands
    • Thompson, J., Reese-Wagoner, A., and Banaszak, L. (1999) Liver fatty acid binding protein: Species variation and the accommodation of different ligands Biochim. Biophys. Acta 1441, 117-130
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 117
    • Thompson, J.1    Reese-Wagoner, A.2    Banaszak, L.3
  • 42
  • 43
    • 18144394277 scopus 로고    scopus 로고
    • Are acidic and basic groups in buried proteins predicted to be ionized?
    • Kim, J., Mao, J., and Gunner, M. R. (2005) Are acidic and basic groups in buried proteins predicted to be ionized? J. Mol. Biol. 348, 1283-1298
    • (2005) J. Mol. Biol. , vol.348 , pp. 1283
    • Kim, J.1    Mao, J.2    Gunner, M.R.3
  • 44
    • 0037297401 scopus 로고    scopus 로고
    • Insights into the bile acid transportation system: The human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures
    • Kurz, M., Brachvogel, V., Matter, H., Stengelin, S., Thuring, H., and Kramer, W. (2003) Insights into the bile acid transportation system: The human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures Proteins 50, 312-328
    • (2003) Proteins , vol.50 , pp. 312
    • Kurz, M.1    Brachvogel, V.2    Matter, H.3    Stengelin, S.4    Thuring, H.5    Kramer, W.6
  • 45
    • 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., and Yan, H. (1998) NMR solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding Biochemistry 37, 12727-12736
    • (1998) Biochemistry , vol.37 , pp. 12727
    • Wang, L.1    Li, Y.2    Abildgaard, F.3    Markley, J.L.4    Yan, H.5
  • 46
    • 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
    • Hodsdon, M. E. and Cistola, D. P. (1997) Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry Biochemistry 36, 1450-1460
    • (1997) Biochemistry , vol.36 , pp. 1450
    • Hodsdon, M.E.1    Cistola, D.P.2


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