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Volumn 386, Issue 2, 2009, Pages 366-378

Homodimeric Chicken Galectin CG-1B (C-14): Crystal Structure and Detection of Unique Redox-Dependent Shape Changes Involving Inter- and Intrasubunit Disulfide Bridges by Gel Filtration, Ultracentrifugation, Site-Directed Mutagenesis, and Peptide Mass Fingerprinting

Author keywords

disulfide bonding; homology; lectin; phylogeny; protein dimerization

Indexed keywords

CHICKEN GALECTIN 1A; CHICKEN GALECTIN 1B; CYSTEINE; DISULFIDE; GALECTIN; HOMODIMER; UNCLASSIFIED DRUG; WATER;

EID: 59149090057     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.09.054     Document Type: Article
Times cited : (35)

References (48)
  • 1
    • 59149092379 scopus 로고    scopus 로고
    • The Sugar Code
    • Gabius H.-J. (Ed), Wiley-VCH, Weinheim
    • Gabius H.-J. The Sugar Code. In: Gabius H.-J. (Ed). Fundamentals of Glycosciences (2009), Wiley-VCH, Weinheim
    • (2009) Fundamentals of Glycosciences
    • Gabius, H.-J.1
  • 2
    • 0035208055 scopus 로고    scopus 로고
    • Towards defining the role of glycans as hardware in information storage and transfer: basic principles, experimental approaches and recent progress
    • Solís D., Jiménez-Barbero J., Kaltner H., Romero A., Siebert H.C., von der Lieth C.W., and Gabis H.-J. Towards defining the role of glycans as hardware in information storage and transfer: basic principles, experimental approaches and recent progress. Cells Tissues Organs 168 (2001) 5-23
    • (2001) Cells Tissues Organs , vol.168 , pp. 5-23
    • Solís, D.1    Jiménez-Barbero, J.2    Kaltner, H.3    Romero, A.4    Siebert, H.C.5    von der Lieth, C.W.6    Gabis, H.-J.7
  • 3
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper D.N. Galectinomics: finding themes in complexity. Biochim. Biophys. Acta 1572 (2002) 209-231
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.1
  • 5
    • 33646554216 scopus 로고    scopus 로고
    • A guide to signaling pathways connecting protein-glycan interaction with the emerging versatile effector functionality of mammalian lectins
    • Villalobo A., Nogales-González A., and Gabius H.-J. A guide to signaling pathways connecting protein-glycan interaction with the emerging versatile effector functionality of mammalian lectins. Trends Glycosci. Glycotechnol. 18 (2006) 1-37
    • (2006) Trends Glycosci. Glycotechnol. , vol.18 , pp. 1-37
    • Villalobo, A.1    Nogales-González, A.2    Gabius, H.-J.3
  • 6
    • 38749099077 scopus 로고    scopus 로고
    • Prototype chicken galectins revisited: characterization of a third protein with distinctive hydrodynamic behaviour and expression pattern in organs of adult animals
    • Kaltner H., Solís D., Kopitz J., Lensch M., Lohr M., Manning J.C., et al. Prototype chicken galectins revisited: characterization of a third protein with distinctive hydrodynamic behaviour and expression pattern in organs of adult animals. Biochem. J. 409 (2008) 591-599
    • (2008) Biochem. J. , vol.409 , pp. 591-599
    • Kaltner, H.1    Solís, D.2    Kopitz, J.3    Lensch, M.4    Lohr, M.5    Manning, J.C.6
  • 7
    • 0033607322 scopus 로고    scopus 로고
    • The 2.15 A crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin
    • Varela P.F., Solís D., Diaz-Mauriño T., Kaltner H., Gabius H.-J., and Romero A. The 2.15 A crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin. J. Mol. Biol. 294 (1999) 537-549
    • (1999) J. Mol. Biol. , vol.294 , pp. 537-549
    • Varela, P.F.1    Solís, D.2    Diaz-Mauriño, T.3    Kaltner, H.4    Gabius, H.-J.5    Romero, A.6
  • 8
    • 0025642403 scopus 로고
    • Structure of chicken 16-kDa beta-galactoside-binding lectin. Complete amino acid sequence, cloning of cDNA, and production of recombinant lectin
    • Sakakura Y., Hirabayashi J., Oda Y., Ohyama Y., and Kasai K. Structure of chicken 16-kDa beta-galactoside-binding lectin. Complete amino acid sequence, cloning of cDNA, and production of recombinant lectin. J. Biol. Chem. 265 (1990) 21573-21579
    • (1990) J. Biol. Chem. , vol.265 , pp. 21573-21579
    • Sakakura, Y.1    Hirabayashi, J.2    Oda, Y.3    Ohyama, Y.4    Kasai, K.5
  • 9
    • 0023304892 scopus 로고
    • Complete amino acid sequence of 14 kDa beta-galactoside-binding lectin of chick embryo
    • Hirabayashi J., Kawasaki H., Suzuki K., and Kasai K. Complete amino acid sequence of 14 kDa beta-galactoside-binding lectin of chick embryo. J. Biochem. 101 (1987) 775-787
    • (1987) J. Biochem. , vol.101 , pp. 775-787
    • Hirabayashi, J.1    Kawasaki, H.2    Suzuki, K.3    Kasai, K.4
  • 10
    • 0026753050 scopus 로고
    • Changes in expression of the endogenous beta-galactoside-binding 14-kDa lectin of chick embryonic skin during epidermal differentiation
    • Akimoto Y., Kawakami H., Oda Y., Obinata A., Endo H., Kasai K., and Hirano H. Changes in expression of the endogenous beta-galactoside-binding 14-kDa lectin of chick embryonic skin during epidermal differentiation. Exp. Cell Res. 199 (1992) 297-304
    • (1992) Exp. Cell Res. , vol.199 , pp. 297-304
    • Akimoto, Y.1    Kawakami, H.2    Oda, Y.3    Obinata, A.4    Endo, H.5    Kasai, K.6    Hirano, H.7
  • 11
    • 0028798759 scopus 로고
    • Changes in expression of two endogenous beta-galactoside-binding isolectins in the dermis of chick embryonic skin during development in ovo and in vitro
    • Akimoto Y., Obinata A., Hirabayashi J., Sakakura Y., Endo H., Kasai K., and Hirano H. Changes in expression of two endogenous beta-galactoside-binding isolectins in the dermis of chick embryonic skin during development in ovo and in vitro. Cell Tissue Res. 279 (1995) 3-12
    • (1995) Cell Tissue Res. , vol.279 , pp. 3-12
    • Akimoto, Y.1    Obinata, A.2    Hirabayashi, J.3    Sakakura, Y.4    Endo, H.5    Kasai, K.6    Hirano, H.7
  • 12
    • 7444242675 scopus 로고    scopus 로고
    • Hippocampal neurons and recombinant galectins as tools for systematic carbohydrate structure-function studies in neuronal differentiation
    • Kopitz J., Russwurm R., Kaltner H., André S., Dotti C.G., Gabius H.-J., et al. Hippocampal neurons and recombinant galectins as tools for systematic carbohydrate structure-function studies in neuronal differentiation. Brain Res. Dev. Brain Res. 153 (2004) 189-196
    • (2004) Brain Res. Dev. Brain Res. , vol.153 , pp. 189-196
    • Kopitz, J.1    Russwurm, R.2    Kaltner, H.3    André, S.4    Dotti, C.G.5    Gabius, H.-J.6
  • 13
    • 17544377102 scopus 로고    scopus 로고
    • Different architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivatives
    • Solís D., Romero A., Kaltner H., Gabius H.-J., and Diaz-Mauriño T. Different architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivatives. J. Biol. Chem. 271 (1996) 12744-12748
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Diaz-Mauriño, T.5
  • 14
    • 0035884413 scopus 로고    scopus 로고
    • Carbohydrate specificity of a galectin from chicken liver (CG-16)
    • Wu A.M., Wu J.H., Tsai M.-S., Kaltner H., and Gabius H.-J. Carbohydrate specificity of a galectin from chicken liver (CG-16). Biochem. J. 358 (2001) 529-538
    • (2001) Biochem. J. , vol.358 , pp. 529-538
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.-S.3    Kaltner, H.4    Gabius, H.-J.5
  • 16
    • 33846518464 scopus 로고    scopus 로고
    • Activity-structure correlations in divergent lectin evolution: fine specificity of chicken galectin CG-14 and computational analysis of flexible ligand docking for CG-14 and the closely related CG-16
    • Wu A.M., Singh T., Liu J.H., Krzeminski M., Russwurm R., Siebert H.-C., et al. Activity-structure correlations in divergent lectin evolution: fine specificity of chicken galectin CG-14 and computational analysis of flexible ligand docking for CG-14 and the closely related CG-16. Glycobiology 17 (2007) 165-184
    • (2007) Glycobiology , vol.17 , pp. 165-184
    • Wu, A.M.1    Singh, T.2    Liu, J.H.3    Krzeminski, M.4    Russwurm, R.5    Siebert, H.-C.6
  • 17
    • 9844267959 scopus 로고    scopus 로고
    • Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution
    • Siebert H.-C., Adar R., Arango R., Burchert M., Kaltner H., Kayser G., et al. Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution. Eur. J. Biochem. 249 (1997) 27-38
    • (1997) Eur. J. Biochem. , vol.249 , pp. 27-38
    • Siebert, H.-C.1    Adar, R.2    Arango, R.3    Burchert, M.4    Kaltner, H.5    Kayser, G.6
  • 18
    • 0021113990 scopus 로고
    • Purification and characterization of beta-galactoside-binding lectin from chick embryonic skin
    • Oda Y., and Kasai K. Purification and characterization of beta-galactoside-binding lectin from chick embryonic skin. Biochim. Biophys. Acta 761 (1983) 237-245
    • (1983) Biochim. Biophys. Acta , vol.761 , pp. 237-245
    • Oda, Y.1    Kasai, K.2
  • 19
    • 0025843406 scopus 로고
    • High-performance affinity chromatography of a chick lectin on an adsorbent based on hydrophilic polymer gel
    • Kakita H., Nakamura K., Kato Y., Oda Y., Shimura K., and Kasai K. High-performance affinity chromatography of a chick lectin on an adsorbent based on hydrophilic polymer gel. J. Chromatogr. 543 (1991) 315-326
    • (1991) J. Chromatogr. , vol.543 , pp. 315-326
    • Kakita, H.1    Nakamura, K.2    Kato, Y.3    Oda, Y.4    Shimura, K.5    Kasai, K.6
  • 20
    • 0027412196 scopus 로고
    • ALSCRIPT: a tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6 (1993) 37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 21
    • 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
    • López-Lucendo M.F., Solís D., André S., Hirabayashi J., Kasai K., Kaltner H., et al. 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 (2004) 957-970
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6
  • 22
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution
    • Lobsanov Y.D., Gitt M.A., Leffler H., Barondes S.H., and Rini J.M. X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. J. Biol. Chem. 268 (1993) 27034-27038
    • (1993) J. Biol. Chem. , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.M.5
  • 23
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction
    • Sörme P., Arnoux P., Kahl-Knutsson B., Leffler H., Rini J.M., and Nilsson U.J. Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction. J. Am. Chem. Soc. 127 (2005) 1737-1743
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1737-1743
    • Sörme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 25
    • 0029646108 scopus 로고
    • Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins
    • Leonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J., and Acharya K.R. Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure 3 (1995) 1379-1393
    • (1995) Structure , vol.3 , pp. 1379-1393
    • Leonidas, D.D.1    Elbert, B.L.2    Zhou, Z.3    Leffler, H.4    Ackerman, S.J.5    Acharya, K.R.6
  • 26
    • 4143099262 scopus 로고    scopus 로고
    • Tumor galectinology: insights into the complex network of a family of endogenous lectins
    • Lahm H., André S., Hoeflich A., Kaltner H., Siebert H.-C., Sordat B., et al. Tumor galectinology: insights into the complex network of a family of endogenous lectins. Glycoconj. J. 20 (2004) 227-238
    • (2004) Glycoconj. J. , vol.20 , pp. 227-238
    • Lahm, H.1    André, S.2    Hoeflich, A.3    Kaltner, H.4    Siebert, H.-C.5    Sordat, B.6
  • 27
    • 33846241804 scopus 로고    scopus 로고
    • Discovery of galectin ligands in fully randomized combinatorial one-bead-one-compound (glyco)peptide libraries
    • André S., Maljaars C.E.P., Halkes K.M., Gabius H.-J., and Kamerling J.P. Discovery of galectin ligands in fully randomized combinatorial one-bead-one-compound (glyco)peptide libraries. Bioorg. Med. Chem. Lett. 17 (2007) 793-798
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 793-798
    • André, S.1    Maljaars, C.E.P.2    Halkes, K.M.3    Gabius, H.-J.4    Kamerling, J.P.5
  • 29
    • 0142057134 scopus 로고    scopus 로고
    • Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells
    • Kopitz J., André S., von Reitzenstein C., Versluis K., Kaltner H., Pieters R.J., et al. Homodimeric galectin-7 (p53-induced gene 1) is a negative growth regulator for human neuroblastoma cells. Oncogene 22 (2003) 6277-6288
    • (2003) Oncogene , vol.22 , pp. 6277-6288
    • Kopitz, J.1    André, S.2    von Reitzenstein, C.3    Versluis, K.4    Kaltner, H.5    Pieters, R.J.6
  • 30
    • 0842328412 scopus 로고    scopus 로고
    • Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets
    • André S., Kaltner H., Furuike T., Nishimura S.-I., and Gabius H.-J. Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets. Bioconjug. Chem. 15 (2004) 87-98
    • (2004) Bioconjug. Chem. , vol.15 , pp. 87-98
    • André, S.1    Kaltner, H.2    Furuike, T.3    Nishimura, S.-I.4    Gabius, H.-J.5
  • 32
    • 0034850491 scopus 로고    scopus 로고
    • Probing the cons and pros of lectin-induced immunomodulation: case studies for the mistletoe lectin and galectin-1
    • Gabius H.-J. Probing the cons and pros of lectin-induced immunomodulation: case studies for the mistletoe lectin and galectin-1. Biochimie 83 (2001) 659-666
    • (2001) Biochimie , vol.83 , pp. 659-666
    • Gabius, H.-J.1
  • 33
    • 27744552971 scopus 로고    scopus 로고
    • Galectin-1 interacts with the {alpha}5{beta}1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27
    • Fischer C., Sanchez-Ruderisch H., Welzel M., Wiedenmann B., Sakai T., André S., et al. Galectin-1 interacts with the {alpha}5{beta}1 fibronectin receptor to restrict carcinoma cell growth via induction of p21 and p27. J. Biol. Chem. 280 (2005) 37266-37277
    • (2005) J. Biol. Chem. , vol.280 , pp. 37266-37277
    • Fischer, C.1    Sanchez-Ruderisch, H.2    Welzel, M.3    Wiedenmann, B.4    Sakai, T.5    André, S.6
  • 34
    • 0021684886 scopus 로고
    • Biochemical characterization of endogenous carbohydrate-binding proteins from spontaneous murine rhabdomyosarcoma, mammary adenocarcinoma, and ovarian teratoma
    • Gabius H.-J., Engelhardt R., Rehm S., and Cramer F. Biochemical characterization of endogenous carbohydrate-binding proteins from spontaneous murine rhabdomyosarcoma, mammary adenocarcinoma, and ovarian teratoma. J. Natl. Cancer Inst. 73 (1984) 1349-1357
    • (1984) J. Natl. Cancer Inst. , vol.73 , pp. 1349-1357
    • Gabius, H.-J.1    Engelhardt, R.2    Rehm, S.3    Cramer, F.4
  • 35
    • 0025076613 scopus 로고
    • Influence of type of linkage and spacer on the interaction of beta-galactoside-binding proteins with immobilized affinity ligands
    • Gabius H.-J. Influence of type of linkage and spacer on the interaction of beta-galactoside-binding proteins with immobilized affinity ligands. Anal. Biochem. 189 (1990) 91-94
    • (1990) Anal. Biochem. , vol.189 , pp. 91-94
    • Gabius, H.-J.1
  • 36
    • 0034493286 scopus 로고    scopus 로고
    • Description of a monomeric prototype galectin from the lizard Podarcis hispanica
    • Solís D., López-Lucendo M.I., Leon S., Varela J., and Diaz-Mauriño T. Description of a monomeric prototype galectin from the lizard Podarcis hispanica. Glycobiology 10 (2000) 1325-1331
    • (2000) Glycobiology , vol.10 , pp. 1325-1331
    • Solís, D.1    López-Lucendo, M.I.2    Leon, S.3    Varela, J.4    Diaz-Mauriño, T.5
  • 39
    • 19944431311 scopus 로고    scopus 로고
    • Determination of structural and functional overlap/divergence of five proto-type galectins by analysis of the growth-regulatory interaction with ganglioside GM1 in silico and in vitro on human neuroblastoma cells
    • André S., Kaltner H., Lensch M., Russwurm R., Siebert H.-C., Fallsehr C., et al. Determination of structural and functional overlap/divergence of five proto-type galectins by analysis of the growth-regulatory interaction with ganglioside GM1 in silico and in vitro on human neuroblastoma cells. Int. J. Cancer 114 (2005) 46-57
    • (2005) Int. J. Cancer , vol.114 , pp. 46-57
    • André, S.1    Kaltner, H.2    Lensch, M.3    Russwurm, R.4    Siebert, H.-C.5    Fallsehr, C.6
  • 41
    • 34447097387 scopus 로고    scopus 로고
    • Tumor suppressor p16INK4a-modulator of glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells
    • André S., Sanchez-Ruderisch H., Nakagawa H., Buchholz M., Kopitz J., Forberich P., et al. Tumor suppressor p16INK4a-modulator of glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells. FEBS J. 274 (2007) 3233-3256
    • (2007) FEBS J. , vol.274 , pp. 3233-3256
    • André, S.1    Sanchez-Ruderisch, H.2    Nakagawa, H.3    Buchholz, M.4    Kopitz, J.5    Forberich, P.6
  • 42
    • 48649102319 scopus 로고    scopus 로고
    • Calix[n]arene-based glycoclusters: bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins
    • André S., Sansone F., Kaltner H., Casnati A., Kopitz J., Gabius H.-J., and Ungaro R. Calix[n]arene-based glycoclusters: bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins. ChemBioChem 9 (2008) 1649-1661
    • (2008) ChemBioChem , vol.9 , pp. 1649-1661
    • André, S.1    Sansone, F.2    Kaltner, H.3    Casnati, A.4    Kopitz, J.5    Gabius, H.-J.6    Ungaro, R.7
  • 43
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. Sect. D 62 (2006) 48-57
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 46
  • 47
    • 28444497752 scopus 로고    scopus 로고
    • Monomer/dimer equilibrium of the AB-type lectin from mistletoe enables combination of toxin/agglutinin activities in one protein: analysis of native and citraconylated proteins by ultracentrifugation/gel filtration and cell biological consequences of dimer destabilization
    • Jimenez M., Saiz J.L., André S., Gabius H.-J., and Solís D. Monomer/dimer equilibrium of the AB-type lectin from mistletoe enables combination of toxin/agglutinin activities in one protein: analysis of native and citraconylated proteins by ultracentrifugation/gel filtration and cell biological consequences of dimer destabilization. Glycobiology 15 (2005) 1386-1395
    • (2005) Glycobiology , vol.15 , pp. 1386-1395
    • Jimenez, M.1    Saiz, J.L.2    André, S.3    Gabius, H.-J.4    Solís, D.5


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