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Volumn 71, Issue 1, 2008, Pages 426-439

N-linked glycans of the human insulin receptor and their distribution over the crystal structure

Author keywords

Glycopeptides; Glycoprotein; Mass spectrometry; Molecular modelling; Three dimensional structure

Indexed keywords

AMINO ACID; BINDING PROTEIN; DIMER; GLYCAN DERIVATIVE; GLYCOPEPTIDE; GLYCOSYLATED PROTEIN; HUMAN INSULIN; IMMUNOGLOBULIN F(AB) FRAGMENT; INSULIN RECEPTOR; MANNOSE; PROTEINASE; RECEPTOR ANTIBODY;

EID: 40549117199     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21768     Document Type: Article
Times cited : (63)

References (48)
  • 3
    • 0031733824 scopus 로고
    • Lectins as chaperones in glycoprotein folding
    • Trombetta ES, Helenius A. Lectins as chaperones in glycoprotein folding. Curr Opin Struct Biol 1990;8:587-592.
    • (1990) Curr Opin Struct Biol , vol.8 , pp. 587-592
    • Trombetta, E.S.1    Helenius, A.2
  • 4
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • Bass J, Chiu G, Argon Y, Steiner DF. Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J Cell Biol 1998;141:637-646.
    • (1998) J Cell Biol , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 5
  • 6
    • 0033906634 scopus 로고    scopus 로고
    • Structure and function of the type I insulin-like growth factor receptor
    • Adams TE, Epa VC, Garrett TPJ, Ward CW. Structure and function of the type I insulin-like growth factor receptor. Cell Mol Life Sci 2000;57:1050-1093.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1050-1093
    • Adams, T.E.1    Epa, V.C.2    Garrett, T.P.J.3    Ward, C.W.4
  • 9
    • 0022639709 scopus 로고
    • Mechanism of galactosylation in the golgi apparatus. A Chinese hamster ovary cell mutant deficient in translocation of UDP-galactose across golgi vesicle membranes
    • Deutscher SL, Hirschberg CB. Mechanism of galactosylation in the golgi apparatus. A Chinese hamster ovary cell mutant deficient in translocation of UDP-galactose across golgi vesicle membranes. J Biol Chem 1986;261:96-100.
    • (1986) J Biol Chem , vol.261 , pp. 96-100
    • Deutscher, S.L.1    Hirschberg, C.B.2
  • 11
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek RA. Glycobiology: toward understanding the function of sugars. Chem Rev 1996;96:683-720.
    • (1996) Chem Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 14
    • 0030451064 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of sialylated glycopeptides and proteins using 2,6-dihydroxyacetophenone as a matrix
    • Pitt JJ, Gorman JJ. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of sialylated glycopeptides and proteins using 2,6-dihydroxyacetophenone as a matrix. Rapid Commun Mass Spectrom 1996;10:1786-1788.
    • (1996) Rapid Commun Mass Spectrom , vol.10 , pp. 1786-1788
    • Pitt, J.J.1    Gorman, J.J.2
  • 15
    • 0031570304 scopus 로고    scopus 로고
    • Oligosaccharide characterization and quantitation using 1-phenyl-3-methyl-5-pyrazolone derivatization and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Pitt JJ, Gorman JJ. Oligosaccharide characterization and quantitation using 1-phenyl-3-methyl-5-pyrazolone derivatization and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Biochem 1997;248:63-75.
    • (1997) Anal Biochem , vol.248 , pp. 63-75
    • Pitt, J.J.1    Gorman, J.J.2
  • 16
    • 33747584896 scopus 로고    scopus 로고
    • Crystal structure of the first three domains of the human insulin receptor reveals major differences from the IGF-1 receptor in the regions governing ligand specificity
    • Lou M-Z, Garrett TPJ, Epa VC, McKern NM, Hoyne PA, Bentley JD, Lovrecz GO, Cosgrove LJ, Ward CW. Crystal structure of the first three domains of the human insulin receptor reveals major differences from the IGF-1 receptor in the regions governing ligand specificity. Proc Natl Acad Sci USA 2006;103:12429-12434.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12429-12434
    • Lou, M.-Z.1    Garrett, T.P.J.2    Epa, V.C.3    McKern, N.M.4    Hoyne, P.A.5    Bentley, J.D.6    Lovrecz, G.O.7    Cosgrove, L.J.8    Ward, C.W.9
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0034503620 scopus 로고    scopus 로고
    • CONSCRIPT: A program for generating electron density isosurfaces from Fourier syntheses in protein crystallography
    • Lawrence MC, Bourke P. CONSCRIPT: a program for generating electron density isosurfaces from Fourier syntheses in protein crystallography. J Appl Crystallogr 2000;33:990-991.
    • (2000) J Appl Crystallogr , vol.33 , pp. 990-991
    • Lawrence, M.C.1    Bourke, P.2
  • 20
    • 23144441143 scopus 로고    scopus 로고
    • GlyProt: In silico glycosylation of proteins
    • Web Server Issue:W214-219
    • Bohne-Lang A, von der Lieth CW. GlyProt: in silico glycosylation of proteins. Nucl Acids Res 2005;33 (Web Server Issue):W214-219.
    • (2005) Nucl Acids Res , pp. 33
    • Bohne-Lang, A.1    von der Lieth, C.W.2
  • 22
    • 13444283836 scopus 로고    scopus 로고
    • Carbohydrate Structure Suite (CSS): Analysis of carbohydrate 3D structures derived from the PDB
    • Database Issue:D242-D246
    • Lütteke T, Frank M, von der Lieth CW. Carbohydrate Structure Suite (CSS): analysis of carbohydrate 3D structures derived from the PDB. Nucleic Acids Res 2005;33 (Database Issue):D242-D246.
    • (2005) Nucleic Acids Res , pp. 33
    • Lütteke, T.1    Frank, M.2    von der Lieth, C.W.3
  • 23
    • 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;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly ML. Analytical molecular surface calculation. J Appl Crystallogr 1983;16:548-558.
    • (1983) J Appl Crystallogr , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 25
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 1996;38:305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 26
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 1981;20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 27
    • 0026679890 scopus 로고
    • The three-dimensional structure of an intact monoclonal antibody for canine lymphoma
    • Harris LJ, Larson SB, Hasel KW, Day J, Greenwood A, McPherson A. The three-dimensional structure of an intact monoclonal antibody for canine lymphoma. Nature 1992;360:369-372.
    • (1992) Nature , vol.360 , pp. 369-372
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    Day, J.4    Greenwood, A.5    McPherson, A.6
  • 29
    • 0027109248 scopus 로고
    • Strategies in the crystallization of glycoproteiens and protein complexes
    • Stura EA, Nemerow GR, Wilson IA. Strategies in the crystallization of glycoproteiens and protein complexes. J Cryst Growth 1992;122:273-285.
    • (1992) J Cryst Growth , vol.122 , pp. 273-285
    • Stura, E.A.1    Nemerow, G.R.2    Wilson, I.A.3
  • 30
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998;393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 32
    • 0027456631 scopus 로고
    • Expression of soluble recombinant glycoproteins with predefined glycosylation: Application to the crystallization of the T-cell glycoprotein CD2
    • Davis SJ, Puklavec MJ, Ashford DA, Harlos K, Jones EY; Stuart DI, Williams AF. Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2. Protein Eng 1993;6:229-232.
    • (1993) Protein Eng , vol.6 , pp. 229-232
    • Davis, S.J.1    Puklavec, M.J.2    Ashford, D.A.3    Harlos, K.4    Jones, E.Y.5    Stuart, D.I.6    Williams, A.F.7
  • 34
    • 29444447364 scopus 로고    scopus 로고
    • The crystal structure of CREG, a secreted glycoprotein involved in cellular growth and differentiation
    • Sacher M, Di Bacco A, Lunin W, Ye Z, Wagner J, Gill G, Cygler M. The crystal structure of CREG, a secreted glycoprotein involved in cellular growth and differentiation. Proc Natl Acad Sci USA 2005;102:18326-18331.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18326-18331
    • Sacher, M.1    Di Bacco, A.2    Lunin, W.3    Ye, Z.4    Wagner, J.5    Gill, G.6    Cygler, M.7
  • 35
    • 0027109332 scopus 로고
    • Purification, sequence and crystallization of an anti-tissue factor Fab and its use for the crystallization of tissue factor
    • Ruf W, Stura EA, LaPolla RJ, Syed R, Edgington TS, Wilson IA. Purification, sequence and crystallization of an anti-tissue factor Fab and its use for the crystallization of tissue factor. J Cryst Growth 1992;122:253-264.
    • (1992) J Cryst Growth , vol.122 , pp. 253-264
    • Ruf, W.1    Stura, E.A.2    LaPolla, R.J.3    Syed, R.4    Edgington, T.S.5    Wilson, I.A.6
  • 36
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd PM, Dwek RA. Glycosylation: heterogeneity and the 3D structure of proteins. Crit Rev Biochem Mol Biol 1997;32:1-100.
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 39
    • 0032582687 scopus 로고    scopus 로고
    • Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain
    • Haniu M, Arakawa T, Bures EJ, Young Y, Hui JO, Rohde MF, Welcher AA, Horan T. Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain. J Biol Chem 1998;273:28691-28699.
    • (1998) J Biol Chem , vol.273 , pp. 28691-28699
    • Haniu, M.1    Arakawa, T.2    Bures, E.J.3    Young, Y.4    Hui, J.O.5    Rohde, M.F.6    Welcher, A.A.7    Horan, T.8
  • 40
    • 0020491258 scopus 로고
    • Amino acid sequence of the heavy chain of bovine protein C
    • Stenflo J, Fernlund P. Amino acid sequence of the heavy chain of bovine protein C. J Biol Chem 1982;257:12180-12190.
    • (1982) J Biol Chem , vol.257 , pp. 12180-12190
    • Stenflo, J.1    Fernlund, P.2
  • 41
    • 0025297484 scopus 로고
    • Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites
    • Miletich JP, Broze GJ, Jr. Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J Biol Chem 1990;265:11397-11404.
    • (1990) J Biol Chem , vol.265 , pp. 11397-11404
    • Miletich, J.P.1    Broze Jr., G.J.2
  • 43
    • 0033950717 scopus 로고    scopus 로고
    • Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor
    • Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D. Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J Biochem (Tokyo). 2000;127:65-72.
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 65-72
    • Sato, C.1    Kim, J.H.2    Abe, Y.3    Saito, K.4    Yokoyama, S.5    Kohda, D.6
  • 44
    • 0031041235 scopus 로고    scopus 로고
    • The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study
    • Mir-Shekari SY, Ashford DA, Harvey DJ, Dwek RA, Schulze IT. The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study. J Biol Chem 1997;272:4027-4036.
    • (1997) J Biol Chem , vol.272 , pp. 4027-4036
    • Mir-Shekari, S.Y.1    Ashford, D.A.2    Harvey, D.J.3    Dwek, R.A.4    Schulze, I.T.5
  • 46
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK Amstutz P, Pluckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 2005;23:1257-1268.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 47
    • 12844276589 scopus 로고    scopus 로고
    • Schlehuber S, Skerra A. Lipocalins in drug discovery: from natural ligand-binding proteins to 'anticalins'. Drug Discov Today 2005;10:23-33.
    • Schlehuber S, Skerra A. Lipocalins in drug discovery: from natural ligand-binding proteins to 'anticalins'. Drug Discov Today 2005;10:23-33.
  • 48
    • 33645800972 scopus 로고    scopus 로고
    • RNA aptamers: From basic science towards therapy
    • Ulrich H. RNA aptamers: from basic science towards therapy. Handb Exp Pharmacol 2006;173:305-326.
    • (2006) Handb Exp Pharmacol , vol.173 , pp. 305-326
    • Ulrich, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.