메뉴 건너뛰기




Volumn 5, Issue 2, 1996, Pages 240-247

Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models

Author keywords

C type lectins; CD23; comparative modeling; protein structure prediction; receptor ligand interactions; structure comparison

Indexed keywords

CELL SURFACE RECEPTOR; LECTIN; RECEPTOR PROTEIN;

EID: 0030019805     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050207     Document Type: Article
Times cited : (17)

References (35)
  • 2
    • 0028595693 scopus 로고
    • Molecular model of the extracellular lectin-like domain in CD69
    • Bajorath J, Aruffo A. 1994. Molecular model of the extracellular lectin-like domain in CD69. J Biol Chem 269:32451-32463.
    • (1994) J Biol Chem , vol.269 , pp. 32451-32463
    • Bajorath, J.1    Aruffo, A.2
  • 3
    • 0011226783 scopus 로고
    • On the use of minimization from many randomly generated loop structures in modeling antibody combining sites
    • Bajorath J, Fine RM. 1992. On the use of minimization from many randomly generated loop structures in modeling antibody combining sites, Immunomethods 1:137-146.
    • (1992) Immunomethods , vol.1 , pp. 137-146
    • Bajorath, J.1    Fine, R.M.2
  • 4
    • 0027373337 scopus 로고
    • Knowledge-based model building of proteins: Concepts and examples
    • Bajorath J, Stenkamp R, Aruffo A. 1993. Knowledge-based model building of proteins: Concepts and examples. Protein Sci 2:317-334.
    • (1993) Protein Sci , vol.2 , pp. 317-334
    • Bajorath, J.1    Stenkamp, R.2    Aruffo, A.3
  • 5
    • 0029138349 scopus 로고
    • Comparison of a protein model with its X-ray structure: The ligand binding domain of E-selectin
    • Bajorath J, Stenkamp R, Aruffo A. 1995. Comparison of a protein model with its X-ray structure: The ligand binding domain of E-selectin. Bioconjugate Chem 6:3-6.
    • (1995) Bioconjugate Chem , vol.6 , pp. 3-6
    • Bajorath, J.1    Stenkamp, R.2    Aruffo, A.3
  • 6
    • 0026513913 scopus 로고
    • α-Helical coiled-coil stalks in the low-affinity receptor for IgE (Fc∈II/CD23) and related C-type lectins
    • Beavil AJ, Edmeades RL, Gould HJ, Sutton BJ. 1992. α-Helical coiled-coil stalks in the low-affinity receptor for IgE (Fc∈II/CD23) and related C-type lectins. Proc Natl Acad Sci USA 89:753-757.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 753-757
    • Beavil, A.J.1    Edmeades, R.L.2    Gould, H.J.3    Sutton, B.J.4
  • 8
    • 0026558366 scopus 로고
    • Immunoglobulin E-binding site in Fc∈ receptor (Fc∈RII/CD23) identified by homologscanning mutagenesis
    • Bettler B, Texido G, Raggini S, Rüegg D, Hofstetter H. 1992. Immunoglobulin E-binding site in Fc∈ receptor (Fc∈RII/CD23) identified by homologscanning mutagenesis. J Biol Chem 267:185-191.
    • (1992) J Biol Chem , vol.267 , pp. 185-191
    • Bettler, B.1    Texido, G.2    Raggini, S.3    Rüegg, D.4    Hofstetter, H.5
  • 10
    • 0023807627 scopus 로고
    • Structure of antibody hypervariable loops reproduced by a conformational search algorithm
    • Bruccoleri RE, Haber E, Novotny J. 1988. Structure of antibody hypervariable loops reproduced by a conformational search algorithm. Nature 335:564-568.
    • (1988) Nature , vol.335 , pp. 564-568
    • Bruccoleri, R.E.1    Haber, E.2    Novotny, J.3
  • 11
    • 0002948490 scopus 로고
    • Antibody modeling using the conformational search program CONGEN
    • Bruccoleri RE, Novotny J. 1992. Antibody modeling using the conformational search program CONGEN. Immunomethods 1:96-106.
    • (1992) Immunomethods , vol.1 , pp. 96-106
    • Bruccoleri, R.E.1    Novotny, J.2
  • 12
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM. 1986. The relation between the divergence of sequence and structure in proteins. EMBO J 5:823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 14
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate recognition domains in animal lectins
    • Drickamer K. 1988. Two distinct classes of carbohydrate recognition domains in animal lectins. J Biol Chem 263:9557-9560.
    • (1988) J Biol Chem , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 15
    • 0027293871 scopus 로고
    • 2+-dependent carbohydrate recognition domains in animal proteins
    • 2+-dependent carbohydrate recognition domains in animal proteins. Curr Opin Struct Biol 3:393-400.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 393-400
    • Drickamer, K.1
  • 19
    • 0025825544 scopus 로고
    • Immunohistochemical demonstration of CD23 expression on lymphocytes in rheumatoid synovitis
    • Hellen EA, Rowlands DC, Hansel TT, Kitas GD, Crocker J. 1991. Immunohistochemical demonstration of CD23 expression on lymphocytes in rheumatoid synovitis. J Clin Pathol 44:293-296.
    • (1991) J Clin Pathol , vol.44 , pp. 293-296
    • Hellen, E.A.1    Rowlands, D.C.2    Hansel, T.T.3    Kitas, G.D.4    Crocker, J.5
  • 20
    • 0027506074 scopus 로고
    • Interaction of P-selectin (CD62) and its cellular ligand: Analysis of critical residues
    • Hollenbaugh D, Bajorath J, Stenkamp R, Aruffo A. 1993. Interaction of P-selectin (CD62) and its cellular ligand: Analysis of critical residues. Biochemistry 32:2960-2966.
    • (1993) Biochemistry , vol.32 , pp. 2960-2966
    • Hollenbaugh, D.1    Bajorath, J.2    Stenkamp, R.3    Aruffo, A.4
  • 21
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones TA. 1985. Interactive computer graphics: FRODO. Methods Enzymol 115:157-171.
    • (1985) Methods Enzymol , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 23
  • 25
    • 0027500305 scopus 로고
    • Modelling of the carbohydrate recognition domain of human E-selectin
    • Mills A. 1994. Modelling of the carbohydrate recognition domain of human E-selectin. FEBS Lett 319:5-11.
    • (1994) FEBS Lett , vol.319 , pp. 5-11
    • Mills, A.1
  • 26
    • 0027828920 scopus 로고
    • Modeling of the lectin-homology domains of the human and murine low-affinity Fc∈ receptor (Fc∈RII/CD23)
    • Padlan EA, Helm BA. 1993. Modeling of the lectin-homology domains of the human and murine low-affinity Fc∈ receptor (Fc∈RII/CD23). Receptor 3:325-341.
    • (1993) Receptor , vol.3 , pp. 325-341
    • Padlan, E.A.1    Helm, B.A.2
  • 27
    • 0029116531 scopus 로고
    • Marked amelioration of established collagen-induced arthritis by treatment with antibodies to CD23 in vivo
    • Plater-Zyberk C, Bonnefoy JY. 1995. Marked amelioration of established collagen-induced arthritis by treatment with antibodies to CD23 in vivo. Nature Medicine 1:781-785.
    • (1995) Nature Medicine , vol.1 , pp. 781-785
    • Plater-Zyberk, C.1    Bonnefoy, J.Y.2
  • 28
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder JW, Richards FM. 1987. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J Mol Biol 193:775-791.
    • (1987) J Mol Biol , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 29
    • 0026077902 scopus 로고
    • Biology and chemistry of the low affinity IgE receptor (Fc∈RII/CD23)
    • Richards ML, Katz DH. 1991. Biology and chemistry of the low affinity IgE receptor (Fc∈RII/CD23). Crit Rev Immunol 11:65-86.
    • (1991) Crit Rev Immunol , vol.11 , pp. 65-86
    • Richards, M.L.1    Katz, D.H.2
  • 30
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil
    • Sheriff S, Chang CY, Ezekowitz RAB. 1994. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil. Nature Struct Biol 1:789-793.
    • (1994) Nature Struct Biol , vol.1 , pp. 789-793
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.B.3
  • 31
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins Struct Funct Genet 17:355-362.
    • (1993) Proteins Struct Funct Genet , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 32
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis WI, Drickamer K. 1994. Trimeric structure of a C-type mannose-binding protein. Structure 2:1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 33
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K, Hendrickson WA. 1992. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360:127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 34
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis WI, Kahn R, Fourme R, Drickamer K, Hendrickson WA. 1991. Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254:1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.