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Volumn 9, Issue 5, 1999, Pages 578-584

New animal lectin structures

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; GALECTIN; LECTIN; SIALOADHESIN; SOMATOMEDIN B RECEPTOR; TACHYLECTIN; UNCLASSIFIED DRUG;

EID: 0032871411     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00008-1     Document Type: Review
Times cited : (91)

References (49)
  • 2
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius HJ Animal lectins. Eur J Biochem. 243:1997;543-576.
    • (1997) Eur J Biochem , vol.243 , pp. 543-576
    • Gabius, H.J.1
  • 3
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • In this short review, a sequential model for the evolution of glycoprotein biosynthesis and recognition is presented. By distinguishing between core sugars and terminal elaborations, early structural roles for carbohydrates are contrasted with the information-bearing functions found in multicellular organisms.
    • Drickamer K, Taylor ME Evolving views of protein glycosylation. Trends Biochem Sci. 23:1998;321-324. In this short review, a sequential model for the evolution of glycoprotein biosynthesis and recognition is presented. By distinguishing between core sugars and terminal elaborations, early structural roles for carbohydrates are contrasted with the information-bearing functions found in multicellular organisms.
    • (1998) Trends Biochem Sci , vol.23 , pp. 321-324
    • Drickamer, K.1    Taylor, M.E.2
  • 5
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis WI, Drickamer K Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem. 65:1996;441-473.
    • (1996) Annu Rev Biochem , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 6
  • 8
    • 0029731590 scopus 로고    scopus 로고
    • The sialoadhesins - A family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily
    • Kelm S, Schauer R, Crocker PR The sialoadhesins - a family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily. Glycoconj J. 13:1996;913-926.
    • (1996) Glycoconj J , vol.13 , pp. 913-926
    • Kelm, S.1    Schauer, R.2    Crocker, P.R.3
  • 10
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 Å resolution
    • The X-ray crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose is described. Although the structure is very similar to that of a V-set immunoglobulin fold, it shows a number of differences that have adapted it for sialic acid binding. The structure also provides a detailed picture of the interactions mediating sialic acid binding, in particular Trp2, Arg97 and Trp106 residues, which are well conserved among members of the siglec family.
    • May AP, Robinson RC, Vinson M, Crocker PR, Jones EY Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 Å resolution. Mol Cell. 1:1998;719-728. The X-ray crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose is described. Although the structure is very similar to that of a V-set immunoglobulin fold, it shows a number of differences that have adapted it for sialic acid binding. The structure also provides a detailed picture of the interactions mediating sialic acid binding, in particular Trp2, Arg97 and Trp106 residues, which are well conserved among members of the siglec family.
    • (1998) Mol Cell , vol.1 , pp. 719-728
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3    Crocker, P.R.4    Jones, E.Y.5
  • 11
    • 0032146189 scopus 로고    scopus 로고
    • Functional groups of sialic acids involved in binding to siglecs (sialoadhesins) deduced from interactions with synthetic analogues
    • Kelm S, Brossmer R, Isecke R, Gross HJ, Strenge K, Schauer R Functional groups of sialic acids involved in binding to siglecs (sialoadhesins) deduced from interactions with synthetic analogues. Eur J Biochem. 255:1998;663-672.
    • (1998) Eur J Biochem , vol.255 , pp. 663-672
    • Kelm, S.1    Brossmer, R.2    Isecke, R.3    Gross, H.J.4    Strenge, K.5    Schauer, R.6
  • 12
    • 0028276413 scopus 로고
    • Natural ligands of the B cell adhesion molecule CD22 beta can be masked by 9-O-acetylation of sialic acids
    • Sjoberg ER, Powell LD, Klein A, Varki A Natural ligands of the B cell adhesion molecule CD22 beta can be masked by 9-O-acetylation of sialic acids. J Cell Biol. 126:1994;549-562.
    • (1994) J Cell Biol , vol.126 , pp. 549-562
    • Sjoberg, E.R.1    Powell, L.D.2    Klein, A.3    Varki, A.4
  • 13
    • 0028595625 scopus 로고
    • Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22
    • Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22. Glycoconj J. 11:1994;576-585.
    • (1994) Glycoconj J , vol.11 , pp. 576-585
    • Kelm, S.1    Schauer, R.2    Manuguerra, J.C.3    Gross, H.J.4    Crocker, P.R.5
  • 14
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Kelm S, Schauer R Sialic acids in molecular and cellular interactions. Int Rev Cytol. 175:1997;137-240.
    • (1997) Int Rev Cytol , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 15
    • 0030758770 scopus 로고    scopus 로고
    • Binding specificities of the sialoadhesin family of I-type lectins. Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin
    • Collins BE, Kiso M, Hasegawa A, Tropak MB, Roder JC, Crocker PR, Schnaar RL Binding specificities of the sialoadhesin family of I-type lectins. Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin. J Biol Chem. 272:1997;16889-16895.
    • (1997) J Biol Chem , vol.272 , pp. 16889-16895
    • Collins, B.E.1    Kiso, M.2    Hasegawa, A.3    Tropak, M.B.4    Roder, J.C.5    Crocker, P.R.6    Schnaar, R.L.7
  • 16
    • 0032402696 scopus 로고    scopus 로고
    • Glycan specificity of myelin-associated glycoprotein and sialoadhesin deduced from interactions with synthetic oligosaccharides
    • Strenge K, Schauer R, Bovin N, Hasegawa A, Ishida H, Kiso M, Kelm S Glycan specificity of myelin-associated glycoprotein and sialoadhesin deduced from interactions with synthetic oligosaccharides. Eur J Biochem. 258:1998;677-685.
    • (1998) Eur J Biochem , vol.258 , pp. 677-685
    • Strenge, K.1    Schauer, R.2    Bovin, N.3    Hasegawa, A.4    Ishida, H.5    Kiso, M.6    Kelm, S.7
  • 17
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A Sialic acids as ligands in recognition phenomena. FASEB J. 11:1997;248-255.
    • (1997) FASEB J , vol.11 , pp. 248-255
    • Varki, A.1
  • 18
    • 0030953944 scopus 로고    scopus 로고
    • Regulation of myelin-associated glycoprotein binding by sialylated cis-ligands
    • Tropak MB, Roder JC Regulation of myelin-associated glycoprotein binding by sialylated cis-ligands. J Neurochem. 68:1997;1753-1763.
    • (1997) J Neurochem , vol.68 , pp. 1753-1763
    • Tropak, M.B.1    Roder, J.C.2
  • 19
    • 0032560557 scopus 로고    scopus 로고
    • Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes
    • Razi N, Varki A Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes. Proc Natl Acad Sci USA. 95:1998;7469-7474.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7469-7474
    • Razi, N.1    Varki, A.2
  • 20
    • 0033557570 scopus 로고    scopus 로고
    • Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion
    • Barnes YC, Skelton TP, Stamenkovic I, Sgroi DC Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion. Blood. 93:1999;1245-1252.
    • (1999) Blood , vol.93 , pp. 1245-1252
    • Barnes, Y.C.1    Skelton, T.P.2    Stamenkovic, I.3    Sgroi, D.C.4
  • 22
    • 0024364949 scopus 로고
    • Mannose 6-phosphate receptors and lysosomal enzyme targeting
    • Dahms NM, Lobel P, Kornfeld S Mannose 6-phosphate receptors and lysosomal enzyme targeting. J Biol Chem. 264:1989;12115-12118.
    • (1989) J Biol Chem , vol.264 , pp. 12115-12118
    • Dahms, N.M.1    Lobel, P.2    Kornfeld, S.3
  • 23
    • 0029089823 scopus 로고
    • Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes
    • Hille-Rehfeld A Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes. Biochim Biophys Acta. 1241:1995;177-194.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 177-194
    • Hille-Rehfeld, A.1
  • 24
    • 0026352780 scopus 로고
    • The bovine mannose 6-phosphate/insulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region
    • Westlund B, Dahms NM, Kornfeld S The bovine mannose 6-phosphate/insulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region. J Biol Chem. 266:1991;23233-23239.
    • (1991) J Biol Chem , vol.266 , pp. 23233-23239
    • Westlund, B.1    Dahms, N.M.2    Kornfeld, S.3
  • 25
    • 0027471426 scopus 로고
    • The bovine mannose 6-phosphate/insulin-like growth factor II receptor. The role of arginine residues in mannose 6-phosphate binding
    • Dahms NM, Rose PA, Molkentin JD, Zhang Y, Brzycki MA The bovine mannose 6-phosphate/insulin-like growth factor II receptor. The role of arginine residues in mannose 6-phosphate binding. J Biol Chem. 268:1993;5457-5463.
    • (1993) J Biol Chem , vol.268 , pp. 5457-5463
    • Dahms, N.M.1    Rose, P.A.2    Molkentin, J.D.3    Zhang, Y.4    Brzycki, M.A.5
  • 26
    • 0032524316 scopus 로고    scopus 로고
    • Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor
    • The X-ray crystal structure of the extracytoplasmic domain of the cation-dependent mannose 6-phosphate receptor in complex with mannose 6-phosphate is presented. The structure is found to be dimeric, each monomer possessing a fold that is very similar to that of avidin. The complex shows the importance of the 6-phosphate moiety, as well as of a bound manganese ion. A hypothetical model of a high-affinity complex with β-glucuronidase is also presented.
    • Roberts DL, Weix DJ, Dahms NM, Kim JJ Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell. 93:1998;639-648. The X-ray crystal structure of the extracytoplasmic domain of the cation-dependent mannose 6-phosphate receptor in complex with mannose 6-phosphate is presented. The structure is found to be dimeric, each monomer possessing a fold that is very similar to that of avidin. The complex shows the importance of the 6-phosphate moiety, as well as of a bound manganese ion. A hypothetical model of a high-affinity complex with β-glucuronidase is also presented.
    • (1998) Cell , vol.93 , pp. 639-648
    • Roberts, D.L.1    Weix, D.J.2    Dahms, N.M.3    Kim, J.J.4
  • 27
    • 0032497956 scopus 로고    scopus 로고
    • Characterization of truncated and glycosylation-deficient forms of the cation-dependent mannose 6-phosphate receptor expressed in baculovirus-infected insect cells
    • Marron-Terada PG, Bollinger KE, Dahms NM Characterization of truncated and glycosylation-deficient forms of the cation-dependent mannose 6-phosphate receptor expressed in baculovirus-infected insect cells. Biochemistry. 37:1998;17223-17229.
    • (1998) Biochemistry , vol.37 , pp. 17223-17229
    • Marron-Terada, P.G.1    Bollinger, K.E.2    Dahms, N.M.3
  • 28
    • 0032516810 scopus 로고    scopus 로고
    • Protein transport from the secretory to the endocytic pathway in mammalian cells
    • Le Borgne R, Hoflack B Protein transport from the secretory to the endocytic pathway in mammalian cells. Biochim Biophys Acta. 1404:1998;195-209.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 195-209
    • Le Borgne, R.1    Hoflack, B.2
  • 29
    • 0033534489 scopus 로고    scopus 로고
    • The rate of internalization of the mannose 6-phosphate/insulin-like growth factor II receptor is enhanced by multivalent ligand binding
    • Cross-linking of the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR) by β-glucuronidase is found to increase the internalization of the lysosomal enzyme. Receptor dimerization is proposed to promote the incorporation of ligand-bound receptors into clathrin-coated pits.
    • York SJ, Arneson LS, Gregory WT, Dahms NM, Kornfeld S The rate of internalization of the mannose 6-phosphate/insulin-like growth factor II receptor is enhanced by multivalent ligand binding. J Biol Chem. 274:1999;1164-1171. Cross-linking of the insulin-like growth factor II/cation-independent mannose 6-phosphate receptor (IGF-II/CI-MPR) by β-glucuronidase is found to increase the internalization of the lysosomal enzyme. Receptor dimerization is proposed to promote the incorporation of ligand-bound receptors into clathrin-coated pits.
    • (1999) J Biol Chem , vol.274 , pp. 1164-1171
    • York, S.J.1    Arneson, L.S.2    Gregory, W.T.3    Dahms, N.M.4    Kornfeld, S.5
  • 31
    • 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. 269:1994;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
  • 32
    • 0002675139 scopus 로고    scopus 로고
    • Introduction to galectins
    • A very useful review of the galectins, providing information on their classification, structure, carbohydrate-binding properties and functional roles. This article is the first of several found in this special issue devoted to galectins.
    • Leffler H Introduction to galectins. Trends Glycosci Glycotechnol. 9:1997;9-19. A very useful review of the galectins, providing information on their classification, structure, carbohydrate-binding properties and functional roles. This article is the first of several found in this special issue devoted to galectins.
    • (1997) Trends Glycosci Glycotechnol , vol.9 , pp. 9-19
    • Leffler, H.1
  • 33
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain
    • Oda Y, Herrmann J, Gitt MA, Turck CW, Burlingame AL, Barondes SH, Leffler H Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain. J Biol Chem. 268:1993;5929-5939.
    • (1993) J Biol Chem , vol.268 , pp. 5929-5939
    • Oda, Y.1    Herrmann, J.2    Gitt, M.A.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, S.H.6    Leffler, H.7
  • 35
    • 0031903188 scopus 로고    scopus 로고
    • Galectin-7, a marker of all types of stratified epithelia
    • Magnaldo T, Fowlis D, Darmon M Galectin-7, a marker of all types of stratified epithelia. Differentiation. 63:1998;159-168.
    • (1998) Differentiation , vol.63 , pp. 159-168
    • Magnaldo, T.1    Fowlis, D.2    Darmon, M.3
  • 36
    • 0032491184 scopus 로고    scopus 로고
    • Structural basis for the recognition of carbohydrates by human galectin-7
    • The X-ray crystal structure of galectin-7, both free and in complex with galactose, galactosamine, lactose and N-acetyllactosamine, is described. This structure provides the first evidence for a noncanonical carbohydrate-recognition domain arrangement among members of the galectin family.
    • Leonidas DD, Vatzaki EH, Vorum H, Celis JE, Madsen P, Acharya KR Structural basis for the recognition of carbohydrates by human galectin-7. Biochemistry. 37:1998;13930-13940. The X-ray crystal structure of galectin-7, both free and in complex with galactose, galactosamine, lactose and N-acetyllactosamine, is described. This structure provides the first evidence for a noncanonical carbohydrate-recognition domain arrangement among members of the galectin family.
    • (1998) Biochemistry , vol.37 , pp. 13930-13940
    • Leonidas, D.D.1    Vatzaki, E.H.2    Vorum, H.3    Celis, J.E.4    Madsen, P.5    Acharya, K.R.6
  • 37
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-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 2.9-Å 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
  • 38
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein
    • Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proc Natl Acad Sci USA. 91:1994;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
  • 39
    • 0028855759 scopus 로고
    • Identification of galectin-3 as a factor in pre-mRNA splicing
    • Dagher SF, Wang JL, Patterson RJ Identification of galectin-3 as a factor in pre-mRNA splicing. Proc Natl Acad Sci USA. 92:1995;1213-1217.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1213-1217
    • Dagher, S.F.1    Wang, J.L.2    Patterson, R.J.3
  • 40
    • 0029900083 scopus 로고    scopus 로고
    • Expression of galectin-3 modulates T-cell growth and apoptosis
    • Yang RY, Hsu DK, Liu FT Expression of galectin-3 modulates T-cell growth and apoptosis. Proc Natl Acad Sci USA. 93:1996;6737-6742.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6737-6742
    • Yang, R.Y.1    Hsu, D.K.2    Liu, F.T.3
  • 41
    • 0028984238 scopus 로고
    • Galectin-3 expression and effects on cyst enlargement and tubulogenesis in kidney epithelial MDCK cells cultured in three-dimensional matrices in vitro
    • Bao Q, Hughes RC Galectin-3 expression and effects on cyst enlargement and tubulogenesis in kidney epithelial MDCK cells cultured in three-dimensional matrices in vitro. J Cell Sci. 108:1995;2791-2800.
    • (1995) J Cell Sci , vol.108 , pp. 2791-2800
    • Bao, Q.1    Hughes, R.C.2
  • 42
    • 0027422375 scopus 로고
    • Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase
    • Herrmann J, Turck CW, Atchison RE, Huflejt ME, Poulter L, Gitt MA, Burlingame AL, Barondes SH, Leffler H Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase. J Biol Chem. 268:1993;26704-26711.
    • (1993) J Biol Chem , vol.268 , pp. 26704-26711
    • Herrmann, J.1    Turck, C.W.2    Atchison, R.E.3    Huflejt, M.E.4    Poulter, L.5    Gitt, M.A.6    Burlingame, A.L.7    Barondes, S.H.8    Leffler, H.9
  • 43
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution
    • This paper describes the X-ray crystal structure of the carbohydrate-recognition domain (CRD) from galectin-3 in complex with N-acetyllactosamine. The structure shows that the canonical galectin-1/-2 dimer interface has been eliminated, but that a second mode of CRD-CRD interaction may be possible. In addition, the structure provides insight into the basis of its oligosaccharide- and RNA-binding properties.
    • 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. 273:1998;13047-13052. This paper describes the X-ray crystal structure of the carbohydrate-recognition domain (CRD) from galectin-3 in complex with N-acetyllactosamine. The structure shows that the canonical galectin-1/-2 dimer interface has been eliminated, but that a second mode of CRD-CRD interaction may be possible. In addition, the structure provides insight into the basis of its oligosaccharide- and RNA-binding properties.
    • (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
  • 44
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga S, Kawabata S, Muta T New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem (Tokyo). 123:1998;1-15.
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 45
    • 0029611240 scopus 로고
    • Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes
    • Okino N, Kawabata S, Saito T, Hirata M, Takagi T, Iwanaga S Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J Biol Chem. 270:1995;31008-31015.
    • (1995) J Biol Chem , vol.270 , pp. 31008-31015
    • Okino, N.1    Kawabata, S.2    Saito, T.3    Hirata, M.4    Takagi, T.5    Iwanaga, S.6
  • 46
    • 0033522446 scopus 로고    scopus 로고
    • Tachylectin 2: Crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
    • The X-ray crystal structure of tachylectin-2 in complex with N-acetylglucosamine (GlcNAc) is described. The structure reveals a new lectin fold and is the first example of a five-bladed β-propeller protein. The planar arrangement of five carbohydrate-binding sites is consistent with a role in binding the terminal GlcNAc moieties typical of certain Gram-positive bacteria.
    • Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W Tachylectin 2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J. 18:1999;2313-2322. The X-ray crystal structure of tachylectin-2 in complex with N-acetylglucosamine (GlcNAc) is described. The structure reveals a new lectin fold and is the first example of a five-bladed β-propeller protein. The planar arrangement of five carbohydrate-binding sites is consistent with a role in binding the terminal GlcNAc moieties typical of certain Gram-positive bacteria.
    • (1999) EMBO J , vol.18 , pp. 2313-2322
    • Beisel, H.G.1    Kawabata, S.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 47
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • The roles of various C-type lectins in the immune system are reviewed. Emphasis is placed on explaining how saccharide-binding specificity, in conjunction with the geometrical arrangement of carbohydrate-recognition domains, dictates function.
    • Weis WI, Taylor ME, Drickamer K The C-type lectin superfamily in the immune system. Immunol Rev. 163:1998;19-34. The roles of various C-type lectins in the immune system are reviewed. Emphasis is placed on explaining how saccharide-binding specificity, in conjunction with the geometrical arrangement of carbohydrate-recognition domains, dictates function.
    • (1998) Immunol Rev , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 48
    • 0031817313 scopus 로고    scopus 로고
    • CD2 and the nature of protein interactions mediating cell-cell recognition
    • A detailed analysis of the role played by CD2 and its ligands in mediating cell-cell recognition establishes the importance of weak protein-protein interactions.
    • Davis SJ, Ikemizu S, Wild MK, van der Merwe PA CD2 and the nature of protein interactions mediating cell-cell recognition. Immunol Rev. 163:1998;217-236. A detailed analysis of the role played by CD2 and its ligands in mediating cell-cell recognition establishes the importance of weak protein-protein interactions.
    • (1998) Immunol Rev , vol.163 , pp. 217-236
    • Davis, S.J.1    Ikemizu, S.2    Wild, M.K.3    Van Der Merwe, P.A.4
  • 49
    • 0027609916 scopus 로고
    • SETOR: hardware-lighted three-dimensional solid model representations of macromolecules
    • 127-128
    • Evans SV: SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J Mol Graph 1993, 11:134-138, 127-128.
    • (1993) J Mol Graph , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.