메뉴 건너뛰기




Volumn 34, Issue , 2015, Pages 108-115

Sugar recognition and protein-protein interaction of mammalian lectins conferring diverse functions

Author keywords

[No Author keywords available]

Indexed keywords

AGLYCONE; GLYCAN; LECTIN; SUGAR; CARBOHYDRATE; CARRIER PROTEIN; LIGAND; MEMBRANE PROTEIN; POLYSACCHARIDE; PROTEIN BINDING;

EID: 84942512347     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2015.08.005     Document Type: Review
Times cited : (27)

References (57)
  • 3
    • 84888357760 scopus 로고    scopus 로고
    • Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2
    • Nagae M., Yamanaka K., Hanashima S., Ikeda A., Morita-Matsumoto K., Satoh T., Matsumoto N., Yamamoto K., Yamaguchi Y. Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2. J Biol Chem 2013, 288:33598-33610.
    • (2013) J Biol Chem , vol.288 , pp. 33598-33610
    • Nagae, M.1    Yamanaka, K.2    Hanashima, S.3    Ikeda, A.4    Morita-Matsumoto, K.5    Satoh, T.6    Matsumoto, N.7    Yamamoto, K.8    Yamaguchi, Y.9
  • 4
    • 84914146149 scopus 로고    scopus 로고
    • A platform of C-type lectin-like receptor CLEC-2 for binding O-glycosylated podoplanin and nonglycosylated rhodocytin
    • Nagae M., Morita-Matsumoto K., Kato M., Kaneko M.K., Kato Y., Yamaguchi Y. A platform of C-type lectin-like receptor CLEC-2 for binding O-glycosylated podoplanin and nonglycosylated rhodocytin. Structure 2014, 22:1711-1721.
    • (2014) Structure , vol.22 , pp. 1711-1721
    • Nagae, M.1    Morita-Matsumoto, K.2    Kato, M.3    Kaneko, M.K.4    Kato, Y.5    Yamaguchi, Y.6
  • 7
    • 84874274351 scopus 로고    scopus 로고
    • Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy
    • Li S., Wandel M.P., Li F., Liu Z., He C., Wu J., Shi Y., Randow F. Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy. Sci Signal 2013, 6:ra9.
    • (2013) Sci Signal , vol.6 , pp. ra9
    • Li, S.1    Wandel, M.P.2    Li, F.3    Liu, Z.4    He, C.5    Wu, J.6    Shi, Y.7    Randow, F.8
  • 8
    • 84875908545 scopus 로고    scopus 로고
    • Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
    • Kim B.W., Hong S.B., Kim J.H., Kwon do H., Song H.K. Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8. Nat Commun 2013, 4:1613.
    • (2013) Nat Commun , vol.4 , pp. 1613
    • Kim, B.W.1    Hong, S.B.2    Kim, J.H.3    Kwon do, H.4    Song, H.K.5
  • 10
    • 79960720473 scopus 로고    scopus 로고
    • Glycosylation, galectins and cellular signaling
    • Boscher C., Dennis J.W., Nabi I.R. Glycosylation, galectins and cellular signaling. Curr Opin Cell Biol 2011, 23:383-392.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 383-392
    • Boscher, C.1    Dennis, J.W.2    Nabi, I.R.3
  • 11
    • 84963951278 scopus 로고    scopus 로고
    • Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum
    • Satoh T., Yamaguchi T., Kato K. Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum. Molecules 2015, 20:2475-2491.
    • (2015) Molecules , vol.20 , pp. 2475-2491
    • Satoh, T.1    Yamaguchi, T.2    Kato, K.3
  • 13
    • 84898934328 scopus 로고    scopus 로고
    • Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold
    • Nagae M., Soga K., Morita-Matsumoto K., Hanashima S., Ikeda A., Yamamoto K., Yamaguchi Y. Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold. Glycobiology 2014, 24:368-378.
    • (2014) Glycobiology , vol.24 , pp. 368-378
    • Nagae, M.1    Soga, K.2    Morita-Matsumoto, K.3    Hanashima, S.4    Ikeda, A.5    Yamamoto, K.6    Yamaguchi, Y.7
  • 14
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H., Mitchell D.A., Drickamer K., Weis W.I. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001, 294:2163-2166.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 16
    • 84892666600 scopus 로고    scopus 로고
    • The challenge and promise of glycomics
    • Cummings R.D., Pierce J.M. The challenge and promise of glycomics. Chem Biol 2014, 21:1-15.
    • (2014) Chem Biol , vol.21 , pp. 1-15
    • Cummings, R.D.1    Pierce, J.M.2
  • 17
    • 84893437530 scopus 로고    scopus 로고
    • The neoglycolipid (NGL)-based oligosaccharide microarray system poised to decipher the meta-glycome
    • Palma A.S., Feizi T., Childs R.A., Chai W., Liu Y. The neoglycolipid (NGL)-based oligosaccharide microarray system poised to decipher the meta-glycome. Curr Opin Chem Biol 2014, 18:87-94.
    • (2014) Curr Opin Chem Biol , vol.18 , pp. 87-94
    • Palma, A.S.1    Feizi, T.2    Childs, R.A.3    Chai, W.4    Liu, Y.5
  • 19
    • 84922189307 scopus 로고    scopus 로고
    • Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation
    • Yamaguchi T., Sakae Y., Zhang Y., Yamamoto S., Okamoto Y., Kato K. Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation. Angew Chem Int Ed Engl 2014, 53:10941-10944.
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 10941-10944
    • Yamaguchi, T.1    Sakae, Y.2    Zhang, Y.3    Yamamoto, S.4    Okamoto, Y.5    Kato, K.6
  • 20
    • 0027996135 scopus 로고
    • Structure and energetics of protein carbohydrate complexes
    • Toone E.J. Structure and energetics of protein carbohydrate complexes. Curr Opin Struct Biol 1994, 4:719-728.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 719-728
    • Toone, E.J.1
  • 21
    • 84888384303 scopus 로고    scopus 로고
    • Crystal structure of anti-polysialic acid antibody single chain Fv fragment complexed with octasialic acid: insight into the binding preference for polysialic acid
    • Nagae M., Ikeda A., Hane M., Hanashima S., Kitajima K., Sato C., Yamaguchi Y. Crystal structure of anti-polysialic acid antibody single chain Fv fragment complexed with octasialic acid: insight into the binding preference for polysialic acid. J Biol Chem 2013, 288:33784-33796.
    • (2013) J Biol Chem , vol.288 , pp. 33784-33796
    • Nagae, M.1    Ikeda, A.2    Hane, M.3    Hanashima, S.4    Kitajima, K.5    Sato, C.6    Yamaguchi, Y.7
  • 22
    • 0035852973 scopus 로고    scopus 로고
    • Multivalent protein-carbohydrate interactions. A new paradigm for supermolecular assembly and signal transduction
    • Sacchettini J.C., Baum L.G., Brewer C.F. Multivalent protein-carbohydrate interactions. A new paradigm for supermolecular assembly and signal transduction. Biochemistry 2001, 40:3009-3015.
    • (2001) Biochemistry , vol.40 , pp. 3009-3015
    • Sacchettini, J.C.1    Baum, L.G.2    Brewer, C.F.3
  • 24
    • 84908501531 scopus 로고    scopus 로고
    • Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1
    • Silva-Martín N., Bartual S.G., Ramírez-Aportela E., Chacón P., Park C.G., Hermoso J.A. Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1. Structure 2014, 22:1595-1606.
    • (2014) Structure , vol.22 , pp. 1595-1606
    • Silva-Martín, N.1    Bartual, S.G.2    Ramírez-Aportela, E.3    Chacón, P.4    Park, C.G.5    Hermoso, J.A.6
  • 26
    • 40749122107 scopus 로고    scopus 로고
    • An essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR)
    • Wang J., Shiratori I., Satoh T., Lanier L.L., Arase H. An essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR). J Immunol 2008, 180:1686-1693.
    • (2008) J Immunol , vol.180 , pp. 1686-1693
    • Wang, J.1    Shiratori, I.2    Satoh, T.3    Lanier, L.L.4    Arase, H.5
  • 27
    • 84860875016 scopus 로고    scopus 로고
    • Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands
    • Sun Y., Senger K., Baginski T.K., Mazloom A., Chinn Y., Pantua H., Hamidzadeh K., Ramani S.R., Luis E., Tom I., et al. Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands. J Biol Chem 2012, 287:15837-15850.
    • (2012) J Biol Chem , vol.287 , pp. 15837-15850
    • Sun, Y.1    Senger, K.2    Baginski, T.K.3    Mazloom, A.4    Chinn, Y.5    Pantua, H.6    Hamidzadeh, K.7    Ramani, S.R.8    Luis, E.9    Tom, I.10
  • 29
    • 72849125119 scopus 로고    scopus 로고
    • Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor α depends on specific sialylated O-linked glycans on gB
    • Wang J., Fan Q., Satoh T., Arii J., Lanier L.L., Spear P.G., Kawaguchi Y., Arase H. Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor α depends on specific sialylated O-linked glycans on gB. J Virol 2009, 83:13042-13045.
    • (2009) J Virol , vol.83 , pp. 13042-13045
    • Wang, J.1    Fan, Q.2    Satoh, T.3    Arii, J.4    Lanier, L.L.5    Spear, P.G.6    Kawaguchi, Y.7    Arase, H.8
  • 30
    • 33845948942 scopus 로고    scopus 로고
    • Siglec-7 undergoes a major conformational change when complexed with the α(2,8)-disialylganglioside GT1b
    • Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R., van Aalten D.M. Siglec-7 undergoes a major conformational change when complexed with the α(2,8)-disialylganglioside GT1b. J Biol Chem 2006, 281:32774-32783.
    • (2006) J Biol Chem , vol.281 , pp. 32774-32783
    • Attrill, H.1    Imamura, A.2    Sharma, R.S.3    Kiso, M.4    Crocker, P.R.5    van Aalten, D.M.6
  • 31
    • 77958473336 scopus 로고    scopus 로고
    • Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3
    • Han L., Monné M., Okumura H., Schwend T., Cherry A.L., Flot D., Matsuda T., Jovine L. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3. Cell 2010, 143:404-415.
    • (2010) Cell , vol.143 , pp. 404-415
    • Han, L.1    Monné, M.2    Okumura, H.3    Schwend, T.4    Cherry, A.L.5    Flot, D.6    Matsuda, T.7    Jovine, L.8
  • 32
    • 80053570445 scopus 로고    scopus 로고
    • Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
    • Rana N.A., Haltiwanger R.S. Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors. Curr Opin Struct Biol 2011, 21:583-589.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 583-589
    • Rana, N.A.1    Haltiwanger, R.S.2
  • 34
  • 37
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer K. Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 1992, 360:183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 38
    • 79251601252 scopus 로고    scopus 로고
    • Structural basis for langerin recognition of diverse pathogen and mammalian glycans through a single binding site
    • Feinberg H., Taylor M.E., Razi N., McBride R., Knirel Y.A., Graham S.A., Drickamer K., Weis W.I. Structural basis for langerin recognition of diverse pathogen and mammalian glycans through a single binding site. J Mol Biol 2011, 405:1027-1039.
    • (2011) J Mol Biol , vol.405 , pp. 1027-1039
    • Feinberg, H.1    Taylor, M.E.2    Razi, N.3    McBride, R.4    Knirel, Y.A.5    Graham, S.A.6    Drickamer, K.7    Weis, W.I.8
  • 39
    • 84870586527 scopus 로고    scopus 로고
    • Glycosaminoglycans are interactants of langerin: comparison with gp120 highlights an unexpected calcium-independent binding mode
    • Chabrol E., Nurisso A., Daina A., Vassal-Stermann E., Thepaut M., Girard E., Vivés R.R., Fieschi F. Glycosaminoglycans are interactants of langerin: comparison with gp120 highlights an unexpected calcium-independent binding mode. PLoS ONE 2012, 7:e50722.
    • (2012) PLoS ONE , vol.7 , pp. e50722
    • Chabrol, E.1    Nurisso, A.2    Daina, A.3    Vassal-Stermann, E.4    Thepaut, M.5    Girard, E.6    Vivés, R.R.7    Fieschi, F.8
  • 40
    • 84926300956 scopus 로고    scopus 로고
    • Langerin-heparin interaction: two binding sites for small and large ligands as revealed by a combination of NMR spectroscopy and cross-linking mapping experiments
    • Muñoz-García J.C., Chabrol E., Vivès R.R., Thomas A., de Paz J.L., Rojo J., Imberty A., Fieschi F., Nieto P.M., Angulo J. Langerin-heparin interaction: two binding sites for small and large ligands as revealed by a combination of NMR spectroscopy and cross-linking mapping experiments. J Am Chem Soc 2015, 137:4100-4110.
    • (2015) J Am Chem Soc , vol.137 , pp. 4100-4110
    • Muñoz-García, J.C.1    Chabrol, E.2    Vivès, R.R.3    Thomas, A.4    de Paz, J.L.5    Rojo, J.6    Imberty, A.7    Fieschi, F.8    Nieto, P.M.9    Angulo, J.10
  • 43
    • 84923779003 scopus 로고    scopus 로고
    • Discovery, primary and crystal structures, and capacitation-related properties of a prostate-derived heparin-binding protein WGA16 from boar sperm
    • Garénaux E., Kanagawa M., Tsuchiyama T., Hori K., Kanazawa T., Goshima A., Chiba M., Yasue H., Ikeda A., Yamaguchi Y., et al. Discovery, primary and crystal structures, and capacitation-related properties of a prostate-derived heparin-binding protein WGA16 from boar sperm. J Biol Chem 2015, 290:5484-5501.
    • (2015) J Biol Chem , vol.290 , pp. 5484-5501
    • Garénaux, E.1    Kanagawa, M.2    Tsuchiyama, T.3    Hori, K.4    Kanazawa, T.5    Goshima, A.6    Chiba, M.7    Yasue, H.8    Ikeda, A.9    Yamaguchi, Y.10
  • 44
    • 0032587136 scopus 로고    scopus 로고
    • The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells
    • Kleene R., Dartsch H., Kern H.F. The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells. Eur J Cell Biol 1999, 78:79-90.
    • (1999) Eur J Cell Biol , vol.78 , pp. 79-90
    • Kleene, R.1    Dartsch, H.2    Kern, H.F.3
  • 47
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston T.L., Wandel M.P., von Muhlinen N., Foeglein Á., Randow F. Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 2012, 482:414-418.
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, Á.4    Randow, F.5
  • 49
    • 79953197242 scopus 로고    scopus 로고
    • Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans
    • Ideo H., Matsuzaka T., Nonaka T., Seko A., Yamashita K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem 2011, 286:11346-11355.
    • (2011) J Biol Chem , vol.286 , pp. 11346-11355
    • Ideo, H.1    Matsuzaka, T.2    Nonaka, T.3    Seko, A.4    Yamashita, K.5
  • 53
    • 33748039462 scopus 로고    scopus 로고
    • Symbiotic bacteria direct expression of an intestinal bactericidal lectin
    • Cash H.L., Whitham C.V., Behrendt C.L., Hooper L.V. Symbiotic bacteria direct expression of an intestinal bactericidal lectin. Science 2006, 313:1126-1130.
    • (2006) Science , vol.313 , pp. 1126-1130
    • Cash, H.L.1    Whitham, C.V.2    Behrendt, C.L.3    Hooper, L.V.4
  • 55
    • 0031022383 scopus 로고    scopus 로고
    • Carbohydrate-binding properties of the hemolytic lectin CEL-III from the holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate
    • Hatakeyama T., Miyamoto Y., Nagatomo H., Sallay I., Yamasaki N. Carbohydrate-binding properties of the hemolytic lectin CEL-III from the holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate. J Biochem 1997, 121:63-67.
    • (1997) J Biochem , vol.121 , pp. 63-67
    • Hatakeyama, T.1    Miyamoto, Y.2    Nagatomo, H.3    Sallay, I.4    Yamasaki, N.5
  • 56
    • 84899723735 scopus 로고    scopus 로고
    • Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process
    • Unno H., Goda S., Hatakeyama T. Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process. J Biol Chem 2014, 289:12805-12812.
    • (2014) J Biol Chem , vol.289 , pp. 12805-12812
    • Unno, H.1    Goda, S.2    Hatakeyama, T.3
  • 57
    • 38049101041 scopus 로고    scopus 로고
    • C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type β-trefoil folds
    • Hatakeyama T., Unno H., Kouzuma Y., Uchida T., Eto S., Hidemura H., Kato N., Yonekura M., Kusunoki M. C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type β-trefoil folds. J Biol Chem 2007, 282:37826-37835.
    • (2007) J Biol Chem , vol.282 , pp. 37826-37835
    • Hatakeyama, T.1    Unno, H.2    Kouzuma, Y.3    Uchida, T.4    Eto, S.5    Hidemura, H.6    Kato, N.7    Yonekura, M.8    Kusunoki, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.