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Volumn 49, Issue 35, 2010, Pages 7652-7658

Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL SYSTEMS; DICHROISM; DIMERIZATION; LIGANDS; MOLECULAR DYNAMICS; PROTEINS; SUGARS; THERMODYNAMIC STABILITY;

EID: 77956165265     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100356g     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0003818541 scopus 로고    scopus 로고
    • Structure and Mechanism in Protein Science
    • 1st ed., W. H. Freeman, New York.
    • Fersht, A. (1998) Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding, 1st ed., W. H. Freeman, New York.
    • (1998) A Guide to Enzyme Catalysis and Protein Folding
    • Fersht, A.1
  • 4
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the Carbohydrate Moiety on the Stability of Glycoproteins
    • Wang, C., Eufemi, M., Turano, C., and Giartosio, A. (1996) Influence of the Carbohydrate Moiety on the Stability of Glycoproteins Biochemistry 35, 23
    • (1996) Biochemistry , vol.35 , pp. 23
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 5
    • 41649120211 scopus 로고    scopus 로고
    • Structural and thermodynamic effects of ANS binding to human interleukin-1 receptor antagonist
    • Latypov, R. F., Liu, D., Gunasekaran, K., Harvey, T. S., Razinkov, V. I., and Raibekas, A. A. (2008) Structural and thermodynamic effects of ANS binding to human interleukin-1 receptor antagonist Protein Sci. 17, 652-663
    • (2008) Protein Sci. , vol.17 , pp. 652-663
    • Latypov, R.F.1    Liu, D.2    Gunasekaran, K.3    Harvey, T.S.4    Razinkov, V.I.5    Raibekas, A.A.6
  • 6
    • 0038309550 scopus 로고    scopus 로고
    • Protein stability induced by ligand binding correlates with changes in protein flexibility
    • Celej, M. S., Montich, G. G., and Fidelio, G. (2003) Protein stability induced by ligand binding correlates with changes in protein flexibility Protein Sci. 12, 1496-1506
    • (2003) Protein Sci. , vol.12 , pp. 1496-1506
    • Celej, M.S.1    Montich, G.G.2    Fidelio, G.3
  • 7
    • 0021100265 scopus 로고
    • Thermodynamics of binding of l -arabinose and of d -galactose to the binding protein of Escherichia coli
    • Fukada, H., Sturtevant, J. M., and Quiocho, F. A. (1983) Thermodynamics of binding of l -arabinose and of d -galactose to the binding protein of Escherichia coli J. Biol. Chem. 258, 13193-13198
    • (1983) J. Biol. Chem. , vol.258 , pp. 13193-13198
    • Fukada, H.1    Sturtevant, J.M.2    Quiocho, F.A.3
  • 8
    • 0025281866 scopus 로고
    • Study of strong and ultratight protein interaction using differential scanning calorimetry
    • Brandts, J. F. and Lin, L.-N. (1990) Study of strong and ultratight protein interaction using differential scanning calorimetry Biochemistry 29, 6927-6940
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 9
    • 0025238920 scopus 로고
    • Ligand-induced biphasic protein denaturation
    • Shrake, A. and Ross, P. D. (1990) Ligand-induced biphasic protein denaturation J. Biol. Chem. 265, 5055-5059
    • (1990) J. Biol. Chem. , vol.265 , pp. 5055-5059
    • Shrake, A.1    Ross, P.D.2
  • 10
    • 0026908614 scopus 로고
    • Origin and consequences of ligand-induced multiphasic thermal protein denaturation
    • Shrake, A. and Ross, P. D. (1992) Origin and consequences of ligand-induced multiphasic thermal protein denaturation Biopolymers 32, 925-940
    • (1992) Biopolymers , vol.32 , pp. 925-940
    • Shrake, A.1    Ross, P.D.2
  • 11
    • 8444247834 scopus 로고    scopus 로고
    • Conformational flexibility of avidin: The influence of biotin binding
    • Celej, M. S., Montich, G. G., and Fidelio, G. (2004) Conformational flexibility of avidin: The influence of biotin binding Biochem. Biophys. Res. Commun. 325, 922-927
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 922-927
    • Celej, M.S.1    Montich, G.G.2    Fidelio, G.3
  • 12
    • 33846022722 scopus 로고    scopus 로고
    • Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: Effects of ligand binding
    • Kamerzell, T. J., Unruh, J. R., Johnson, C. K., and Middaugh, C. R. (2006) Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: Effects of ligand binding Biochemistry 45 (51) 15288-15300
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15288-15300
    • Kamerzell, T.J.1    Unruh, J.R.2    Johnson, C.K.3    Middaugh, C.R.4
  • 13
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins: He made so many of them
    • Cooper, D. N. W. and Barondes, S. H. (1999) God must love galectins: He made so many of them Glycobiology 9 (10) 979-984
    • (1999) Glycobiology , vol.9 , Issue.10 , pp. 979-984
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 14
    • 45449112374 scopus 로고    scopus 로고
    • Galectins: Structure, function and therapeutic potential
    • Yang, R. Y., Rabinovich, G. A., and Liu, F. T. (2008) Galectins: Structure, function and therapeutic potential Expert Rev. Mol. Med. 10, e17
    • (2008) Expert Rev. Mol. Med. , vol.10 , pp. 17
    • Yang, R.Y.1    Rabinovich, G.A.2    Liu, F.T.3
  • 16
    • 67349258025 scopus 로고    scopus 로고
    • Turning "sweet" on immunity: Galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich, G. A. and Toscano, M. (2009) Turning "sweet" on immunity: Galectin-glycan interactions in immune tolerance and inflammation Nat. Rev. Immunol. 9 (5) 338-352
    • (2009) Nat. Rev. Immunol. , vol.9 , Issue.5 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.2
  • 17
    • 69049116053 scopus 로고    scopus 로고
    • Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1 driven immunoregulatory circuit involving interleukin 27 and interleukin 10
    • Ilarregui, J. M., Croci, D. O., Bianco, G. A., Toscano, M., Salatino, M., Vermeulen, M. E., Greffner, J. R., and Rabinovich, G. A. (2009) Tolerogenic signals delivered by dendritic cells to T cells through a galectin-1 driven immunoregulatory circuit involving interleukin 27 and interleukin 10 Nat. Immunol. 10 (9) 981-991
    • (2009) Nat. Immunol. , vol.10 , Issue.9 , pp. 981-991
    • Ilarregui, J.M.1    Croci, D.O.2    Bianco, G.A.3    Toscano, M.4    Salatino, M.5    Vermeulen, M.E.6    Greffner, J.R.7    Rabinovich, G.A.8
  • 18
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • Lopez-Lucendo, M. F., Solis, D., Andre, S., Hirabayashi, J., Kasai, K., Kaltner, H., Gabius, H. J., and Romero, A. (2004) Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding J. Mol. Biol. 343 (4) 957-970
    • (2004) J. Mol. Biol. , vol.343 , Issue.4 , pp. 957-970
    • Lopez-Lucendo, M.F.1    Solis, D.2    Andre, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6    Gabius, H.J.7    Romero, A.8
  • 19
    • 0141704154 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Galectin-1-oligosaccharides Complexes Reveal the Molecular Basis of Ligand Diversity
    • Ford, M. G., Weimar, T., Kölhi, T., and Woods, R. J. (2003) Molecular Dynamics Simulations of Galectin-1-oligosaccharides Complexes Reveal the Molecular Basis of Ligand Diversity Proteins: Struct., Funct., Genet. 53, 229-240
    • (2003) Proteins: Struct., Funct., Genet. , vol.53 , pp. 229-240
    • Ford, M.G.1    Weimar, T.2    Kölhi, T.3    Woods, R.J.4
  • 20
    • 34547294822 scopus 로고    scopus 로고
    • Characterization of the Carbohydrate Recognition Domain of Galectin-1 in Terms of Solvent Occupancy
    • Di Lella, S., Marti, M. A., Alvarez, R. M. S., Estrin, D. A., and Díaz Ricci, J. C. (2007) Characterization of the Carbohydrate Recognition Domain of Galectin-1 in Terms of Solvent Occupancy J. Phys. Chem. B 111, 7360-7366
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7360-7366
    • Di Lella, S.1    Marti, M.A.2    Alvarez, R.M.S.3    Estrin, D.A.4    Díaz Ricci, J.C.5
  • 21
    • 0028986609 scopus 로고
    • Galectin-1, a β-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization
    • Cho, M. and Cummings, R. D. (1995) Galectin-1, a β-galactoside- binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization J. Biol. Chem. 270 (10) 5198-5206
    • (1995) J. Biol. Chem. , vol.270 , Issue.10 , pp. 5198-5206
    • Cho, M.1    Cummings, R.D.2
  • 22
    • 4444329794 scopus 로고    scopus 로고
    • Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3
    • Ahmad, N., Gabius, H., Sabesan, S., Oscarson, S., and Brewer, C. F. (2004) Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3 Glycobiology 14 (9) 817-825
    • (2004) Glycobiology , vol.14 , Issue.9 , pp. 817-825
    • Ahmad, N.1    Gabius, H.2    Sabesan, S.3    Oscarson, S.4    Brewer, C.F.5
  • 24
    • 1542313834 scopus 로고    scopus 로고
    • Galectin-1: A bifunctional regulator of cellular proliferation
    • Scott, K. and Weinberg, C. (2004) Galectin-1: A bifunctional regulator of cellular proliferation Glycoconjugate J. 19 (7-9) 467-477
    • (2004) Glycoconjugate J. , vol.19 , Issue.7-9 , pp. 467-477
    • Scott, K.1    Weinberg, C.2
  • 26
    • 33845958124 scopus 로고    scopus 로고
    • A novel function for galectin-1 at the crossroad of innate and a adaptive immunity: Galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway
    • Barrionuevo, P., Beigier-Bompadre, M., Ilarregui, J. M., Toscano, M., Bianco, G. A., Isturiz, M. A., and Rabinovich, G. A. (2007) A novel function for galectin-1 at the crossroad of innate and a adaptive immunity: Galectin-1 regulates monocyte/macrophage physiology through a nonapoptotic ERK-dependent pathway J. Immunol. 178 (1) 436-445
    • (2007) J. Immunol. , vol.178 , Issue.1 , pp. 436-445
    • Barrionuevo, P.1    Beigier-Bompadre, M.2    Ilarregui, J.M.3    Toscano, M.4    Bianco, G.A.5    Isturiz, M.A.6    Rabinovich, G.A.7
  • 27
    • 0142075256 scopus 로고    scopus 로고
    • Preparation of recombinant human galectin-1 and use in T cell death assays
    • Pace, K. E., Hahn, H. P., and Baum, L. G. (2003) Preparation of recombinant human galectin-1 and use in T cell death assays Methods Enzymol. 363, 499-518
    • (2003) Methods Enzymol. , vol.363 , pp. 499-518
    • Pace, K.E.1    Hahn, H.P.2    Baum, L.G.3
  • 28
    • 0029800459 scopus 로고    scopus 로고
    • Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis
    • Cho, M. and Cummings, R. D. (1996) Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis Biochemistry 35, 13081-13088
    • (1996) Biochemistry , vol.35 , pp. 13081-13088
    • Cho, M.1    Cummings, R.D.2
  • 30
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • Cheatham, T. E., Cieplak, P., and Kollman, P. A. (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat J. Biomol. Struct. Dyn. 16, 845-862
    • (1999) J. Biomol. Struct. Dyn. , vol.16 , pp. 845-862
    • Cheatham, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 31
    • 0035845496 scopus 로고    scopus 로고
    • Solvent interactions determine carbohydrate conformation
    • Kirschner, K. N. and Woods, R. J. (2001) Solvent interactions determine carbohydrate conformation Proc. Natl. Acad. Sci. U.S.A. 98 (19) 10541-10545
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.19 , pp. 10541-10545
    • Kirschner, K.N.1    Woods, R.J.2
  • 34
    • 85047691965 scopus 로고
    • Self-Consistent Field-Theory of Solvent Effects Representation by Continuum Models: Introduction of Desolvation Contribution
    • Constanciel, R. and Contreras, R. (1984) Self-Consistent Field-Theory of Solvent Effects Representation by Continuum Models: Introduction of Desolvation Contribution Theor. Chim. Acta 65, 1-11
    • (1984) Theor. Chim. Acta , vol.65 , pp. 1-11
    • Constanciel, R.1    Contreras, R.2
  • 35
    • 0344778061 scopus 로고
    • Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics
    • Still, W. C., Tempczyrk, A., Hawley, R. C., and Hendrickson, T. (1990) Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics J. Am. Chem. Soc. 112, 6127-6129
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyrk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 36
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter, J. (1993) Estimation of absolute and relative entropies of macromolecules using the covariance matrix Chem. Phys. Lett. 215, 617-621
    • (1993) Chem. Phys. Lett. , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 37
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • Andricioaei, I. and Karplus, M. (2001) On the calculation of entropy from covariance matrices of the atomic fluctuations J. Chem. Phys. 115 (14) 6289-6292
    • (2001) J. Chem. Phys. , vol.115 , Issue.14 , pp. 6289-6292
    • Andricioaei, I.1    Karplus, M.2
  • 39
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Lee Whitmore, B. A. W. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases Biopolymers 89 (5) 392-400
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 392-400
    • Lee Whitmore, B.A.W.1
  • 40
    • 65549103287 scopus 로고    scopus 로고
    • Thermal and chemical unfolding and refolding of a eukaryotic sodium channel
    • Charalambous, K., O'Reilly, A. O., Bullough, P., and Wallace, B. A. (2009) Thermal and chemical unfolding and refolding of a eukaryotic sodium channel Biochim. Biophys. Acta 1788, 1279-1286
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1279-1286
    • Charalambous, K.1    O'Reilly, A.O.2    Bullough, P.3    Wallace, B.A.4
  • 41
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of Proteins by Ligand Binding: Application to Drug Screening and Determination of Unfolding Energetics
    • Waldron, T. T. and Murphy, K. P. (2003) Stabilization of Proteins by Ligand Binding: Application to Drug Screening and Determination of Unfolding Energetics Biochemistry 42, 5058-5064
    • (2003) Biochemistry , vol.42 , pp. 5058-5064
    • Waldron, T.T.1    Murphy, K.P.2
  • 42
    • 34548694529 scopus 로고    scopus 로고
    • A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron-Sulfur Moieties
    • Todorovic, S., Leal, S. S., Salgueiro, C. A., Zebger, I., Hildebrandt, P., Murgida, D. H., and Gomes, C. M. (2007) A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron-Sulfur Moieties Biochemistry 46, 10733-10738
    • (2007) Biochemistry , vol.46 , pp. 10733-10738
    • Todorovic, S.1    Leal, S.S.2    Salgueiro, C.A.3    Zebger, I.4    Hildebrandt, P.5    Murgida, D.H.6    Gomes, C.M.7
  • 43
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic Stability of Carbonic Anhydrase: Measurments of Binding Affinity and Stoichiometry Using ThermoFluor
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic Stability of Carbonic Anhydrase: Measurments of Binding Affinity and Stoichiometry Using ThermoFluor Biochemistry 44, 5258-5266
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4


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