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Volumn 71, Issue 3, 2008, Pages 1582-1588

Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins

Author keywords

Galectin related protein; Glycoprotein; HSPC159; Lectin; X ray diffraction

Indexed keywords

AMINO ACID; ARGININE; ASPARAGINE; GALECTIN; GALECTIN RELATED PROTEIN; HISTIDINE; LECTIN; UNCLASSIFIED DRUG; VALINE;

EID: 42449105716     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22003     Document Type: Article
Times cited : (22)

References (44)
  • 2
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem 1994;269:20807-20810.
    • (1994) J Biol Chem , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 3
    • 33845987092 scopus 로고    scopus 로고
    • Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition
    • Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R. Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition. J Biol Chem 2006;281:35884-35893.
    • (2006) J Biol Chem , vol.281 , pp. 35884-35893
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6    Kato, R.7
  • 4
    • 0029954457 scopus 로고    scopus 로고
    • Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: The relationship between intramolecular disulfide bridges and TGF activity
    • Yamaoka K, Ingendoh A, Tsubuki S, Nagai Y, Sanai Y. Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: the relationship between intramolecular disulfide bridges and TGF activity. J Biochem (Tokyo) 1996;119:878-886.
    • (1996) J Biochem (Tokyo) , vol.119 , pp. 878-886
    • Yamaoka, K.1    Ingendoh, A.2    Tsubuki, S.3    Nagai, Y.4    Sanai, Y.5
  • 6
    • 0030799196 scopus 로고    scopus 로고
    • Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a β-galactoside-binding lectin
    • Rabinovich GA, Modesti NM, Castagna LF, Landa CA, Riera CM, Sotomayor CE. Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a β-galactoside-binding lectin. J Biochem (Tokyo) 1997;122:365-373.
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 365-373
    • Rabinovich, G.A.1    Modesti, N.M.2    Castagna, L.F.3    Landa, C.A.4    Riera, C.M.5    Sotomayor, C.E.6
  • 7
    • 0032577178 scopus 로고    scopus 로고
    • Regulation of cellular adhesion to extracellular matrix proteins by galectin-3
    • Ochieng J, Leite-Browning ML, Warfield P. Regulation of cellular adhesion to extracellular matrix proteins by galectin-3. Biochem Biophys Res Commun 1998;246:788-791.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 788-791
    • Ochieng, J.1    Leite-Browning, M.L.2    Warfield, P.3
  • 8
    • 0031687508 scopus 로고    scopus 로고
    • Lymphocyte triggering via L-selectin leads to enhanced galectin-3-mediated binding to dendritic cells
    • Swarte W, Mebius RE, Joziasse DH, Van den Eijnden DH, Kraal G. Lymphocyte triggering via L-selectin leads to enhanced galectin-3-mediated binding to dendritic cells. Eur J Immunol 1998;28:2864-2871.
    • (1998) Eur J Immunol , vol.28 , pp. 2864-2871
    • Swarte, W.1    Mebius, R.E.2    Joziasse, D.H.3    Van den Eijnden, D.H.4    Kraal, G.5
  • 9
    • 0023718545 scopus 로고
    • Identification of carbohydrate binding protein 35 in heterogeneous nuclear ribonucleoprotein complex
    • Laing JG, Wang JL. Identification of carbohydrate binding protein 35 in heterogeneous nuclear ribonucleoprotein complex. Biochemistry 1988;27:5329-5334.
    • (1988) Biochemistry , vol.27 , pp. 5329-5334
    • Laing, J.G.1    Wang, J.L.2
  • 12
    • 33745301484 scopus 로고    scopus 로고
    • Galectin-1-matured human monocyte-derived dendritic cells have enhanced migration through extracellular matrix
    • Fulcher JA, Hashimi ST, Levroney EL, Pang M, Gurney KB, Baum LG, Lee B. Galectin-1-matured human monocyte-derived dendritic cells have enhanced migration through extracellular matrix. J Immunol 2006;177:216-226.
    • (2006) J Immunol , vol.177 , pp. 216-226
    • Fulcher, J.A.1    Hashimi, S.T.2    Levroney, E.L.3    Pang, M.4    Gurney, K.B.5    Baum, L.G.6    Lee, B.7
  • 13
    • 0030707480 scopus 로고    scopus 로고
    • Galectin-3: A novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family
    • Akahani S, Nangia-Makker P, Inohara H, Kim HR, Raz A. Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family. Cancer Res 1997;57:5272-5276.
    • (1997) Cancer Res , vol.57 , pp. 5272-5276
    • Akahani, S.1    Nangia-Makker, P.2    Inohara, H.3    Kim, H.R.4    Raz, A.5
  • 14
    • 0030940913 scopus 로고    scopus 로고
    • Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes
    • Perillo NL, Uittenbogaart CH, Nguyen JT, Baum LG. Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes. J Exp Med 1997;185:1851-1858.
    • (1997) J Exp Med , vol.185 , pp. 1851-1858
    • Perillo, N.L.1    Uittenbogaart, C.H.2    Nguyen, J.T.3    Baum, L.G.4
  • 15
    • 0030989330 scopus 로고    scopus 로고
    • Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin
    • Wada J, Ota K, Kumar A, Wallner EI, Kanwar YS. Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin. J Clin Invest 1997;99:2452-2461.
    • (1997) J Clin Invest , vol.99 , pp. 2452-2461
    • Wada, J.1    Ota, K.2    Kumar, A.3    Wallner, E.I.4    Kanwar, Y.S.5
  • 17
    • 21844453220 scopus 로고    scopus 로고
    • Characterization of a galactose binding serum lectin from the Indian catfish, Clarias batrachus: Possible involvement of fish lectins in differential recognition of pathogens
    • Dutta S, Sinha B, Bhattacharya B, Chatterjee B, Mazumder S. Characterization of a galactose binding serum lectin from the Indian catfish, Clarias batrachus: possible involvement of fish lectins in differential recognition of pathogens. Comp Biochem Physiol C Toxicol Pharmacol 2005;141:76-84.
    • (2005) Comp Biochem Physiol C Toxicol Pharmacol , vol.141 , pp. 76-84
    • Dutta, S.1    Sinha, B.2    Bhattacharya, B.3    Chatterjee, B.4    Mazumder, S.5
  • 19
    • 0033777862 scopus 로고    scopus 로고
    • Galectins: A new family of regulators of inflammation
    • Liu FT. Galectins: a new family of regulators of inflammation. Clin Immunol 2000;97:79-88.
    • (2000) Clin Immunol , vol.97 , pp. 79-88
    • Liu, F.T.1
  • 20
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi J, Kasai K. The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 1993;3:297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 21
    • 2542591692 scopus 로고    scopus 로고
    • Discovery and characterization of an epithelial-specific galectin in the endometrium that forms crystals in the trophectoderm
    • Gray CA, Adelson DL, Bazer FW, Burghardt RC, Meeusen EN, Spencer TE. Discovery and characterization of an epithelial-specific galectin in the endometrium that forms crystals in the trophectoderm. Proc Natl Acad Sci USA 2004;101:7982-7987.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7982-7987
    • Gray, C.A.1    Adelson, D.L.2    Bazer, F.W.3    Burghardt, R.C.4    Meeusen, E.N.5    Spencer, T.E.6
  • 22
    • 0032852619 scopus 로고    scopus 로고
    • Galectins: An evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy
    • Rabinovich GA. Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. Cell Death Differ 1999;6:711-721.
    • (1999) Cell Death Differ , vol.6 , pp. 711-721
    • Rabinovich, G.A.1
  • 24
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper DN. Galectinomics: finding themes in complexity. Biochim Biophys Acta 2002;1572:209-231.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.1
  • 25
    • 0034663733 scopus 로고    scopus 로고
    • Soluble β-galactosyl- binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes
    • Bianchet MA, Ahmed H, Vasta GR, Amzel LM. Soluble β-galactosyl- binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins 2000;40:378-388.
    • (2000) Proteins , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 26
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O. Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein. Proc Natl Acad Sci USA 1994;91:1428-1432.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 27
    • 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 MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A. 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 2004;343:957-970.
    • (2004) J Mol Biol , vol.343 , 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
  • 29
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin. L-14-II, in complex with lactose at 29-Å resolution
    • Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM. X-ray crystal structure of the human dimeric S-Lac lectin. L-14-II, in complex with lactose at 29-Å resolution. J Biol Chem 1993;268:27034-27038.
    • (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
  • 30
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution
    • Seetharaman J, Kanigsberg A, Slaaby R, Leffler H, Barondes SH, Rini JM. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution. J Biol Chem 1998;273:13047-13052.
    • (1998) J Biol Chem , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 32
    • 0037177882 scopus 로고    scopus 로고
    • Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion
    • Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J Biol Chem 2002;277:14859-14868.
    • (2002) J Biol Chem , vol.277 , pp. 14859-14868
    • Ackerman, S.J.1    Liu, L.2    Kwatia, M.A.3    Savage, M.P.4    Leonidas, D.D.5    Swaminathan, G.J.6    Acharya, K.R.7
  • 34
    • 33646854012 scopus 로고    scopus 로고
    • Zhou D, Sun J, Zhao W, Zhang X, Shi Y, Teng M, Niu L, Dong Y, Liu P Expression, purification, crystallization and preliminary X-ray characterization of the GRP carbohydrate-recognition domain from Homo sapiens. Acta Crystallogr Sect F Struct Biol Cryst Commun 2006;62 (Part 5):474-476.
    • Zhou D, Sun J, Zhao W, Zhang X, Shi Y, Teng M, Niu L, Dong Y, Liu P Expression, purification, crystallization and preliminary X-ray characterization of the GRP carbohydrate-recognition domain from Homo sapiens. Acta Crystallogr Sect F Struct Biol Cryst Commun 2006;62 (Part 5):474-476.
  • 36
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brunger AT. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr D Biol Crystallogr 1993;49 (Part 1):24-36.
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , Issue.PART 1 , pp. 24-36
    • Brunger, A.T.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50 (Part 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47 (Part 2):110-119.
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
  • 41
  • 43
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 44
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988;16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1


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