메뉴 건너뛰기




Volumn 22, Issue 11, 2003, Pages 2692-2703

Glycoprotein hormone receptors: Determinants in leucine-rich repeats responsible for ligand specificity

Author keywords

Duplicated genes; G protein coupled receptors; Glycoprotein hormone receptors; Leucine rich repeats; Molecular dynamics

Indexed keywords

CHORIONIC GONADOTROPIN RECEPTOR; FOLLITROPIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; GLYCOPROTEIN; LEUCINE; LUTEINIZING HORMONE RECEPTOR; THYROTROPIN RECEPTOR;

EID: 0038182549     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg260     Document Type: Article
Times cited : (181)

References (46)
  • 1
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor, a 2002 perspective
    • Ascoli, M., Fanelli, F. and Segaloff, D.L. (2002) The lutropin/choriogonadotropin receptor, a 2002 perspective. Endocr. Rev., 23, 141-174.
    • (2002) Endocr. Rev. , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 2
    • 0029757509 scopus 로고    scopus 로고
    • Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling
    • Bhowmick, N., Huang, J., Puett, D., Isaacs, N.W. and Lapthorn, A.J. (1996) Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling. Mol. Endocrinol., 10, 1147-1159.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1147-1159
    • Bhowmick, N.1    Huang, J.2    Puett, D.3    Isaacs, N.W.4    Lapthorn, A.J.5
  • 3
    • 0033304846 scopus 로고    scopus 로고
    • Identification of ionizable amino acid residues on the extracellular domain of the lutropin receptor involved in ligand binding
    • Bhowmick, N., Narayan, P. and Puett, D. (1999) Identification of ionizable amino acid residues on the extracellular domain of the lutropin receptor involved in ligand binding. Endocrinology, 140, 4558-4563.
    • (1999) Endocrinology , vol.140 , pp. 4558-4563
    • Bhowmick, N.1    Narayan, P.2    Puett, D.3
  • 4
    • 0025847496 scopus 로고
    • Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity
    • Braun, T., Schofield, P.R. and Sprengel, R. (1991) Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity. EMBO J., 10, 1885-1890.
    • (1991) EMBO J. , vol.10 , pp. 1885-1890
    • Braun, T.1    Schofield, P.R.2    Sprengel, R.3
  • 6
    • 0031003340 scopus 로고    scopus 로고
    • Chimeric proteins can exceed the sum of their parts: Implications for evolution and protein design
    • Campbell, R.K., Bergert, E.R., Wang, Y., Morris, J.C. and Moyle, W.R. (1997) Chimeric proteins can exceed the sum of their parts: implications for evolution and protein design. Nat. Biotechnol., 15, 439-443.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 439-443
    • Campbell, R.K.1    Bergert, E.R.2    Wang, Y.3    Morris, J.C.4    Moyle, W.R.5
  • 7
    • 0031052474 scopus 로고    scopus 로고
    • Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A
    • Chen, C.Z. and Shapiro, R. (1997) Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A. Proc. Natl Acad. Sci. USA, 94, 1761-1766.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1761-1766
    • Chen, C.Z.1    Shapiro, R.2
  • 8
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. and Wells, J.A. (1995) A hot spot of binding energy in a hormone-receptor interface. Science, 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 9
    • 0035928771 scopus 로고    scopus 로고
    • Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor
    • Cornelis, S., Uttenweiler-Joseph, S., Panneels, V., Vassart, G. and Costagliola, S. (2001) Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor. Biochemistry, 40, 9860-9869.
    • (2001) Biochemistry , vol.40 , pp. 9860-9869
    • Cornelis, S.1    Uttenweiler-Joseph, S.2    Panneels, V.3    Vassart, G.4    Costagliola, S.5
  • 10
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids and organic molecules
    • Cornell, W.D. (1995) A second generation force field for the simulation of proteins, nucleic acids and organic molecules. J. Am. Chem. Soc., 117, 5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1
  • 11
    • 0031756989 scopus 로고    scopus 로고
    • Production of bioactive amino-terminal domain of the thyrotropin receptor via insertion in the plasma membrane by a glycosylphosphatidylinositol anchor
    • Costagliola, S., Khoo, D. and Vassart, G. (1998) Production of bioactive amino-terminal domain of the thyrotropin receptor via insertion in the plasma membrane by a glycosylphosphatidylinositol anchor. FEBS Lett., 436, 427-433.
    • (1998) FEBS Lett. , vol.436 , pp. 427-433
    • Costagliola, S.1    Khoo, D.2    Vassart, G.3
  • 12
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T., York, D. and Pedersen, L. (1993) Particle mesh Ewald: An N log(N) method for Ewald sums in large systems. J. Chem. Phys., 98, 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 13
    • 0035668921 scopus 로고    scopus 로고
    • Structural biology of human follitropin and its receptor
    • Dias, J.A. and Van Roey, P. (2001) Structural biology of human follitropin and its receptor. Arch. Med. Res., 32, 510-519.
    • (2001) Arch. Med. Res. , vol.32 , pp. 510-519
    • Dias, J.A.1    Van Roey, P.2
  • 14
    • 0027999473 scopus 로고
    • Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin
    • Dias, J.A., Zhang, Y. and Liu, X. (1994) Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin. J. Biol. Chem., 269, 25289-25294.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25289-25294
    • Dias, J.A.1    Zhang, Y.2    Liu, X.3
  • 15
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack, R.L., Jr and Cohen, F.E. (1997) Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci., 6, 1661-1681.
    • (1997) Protein Sci. , vol.6 , pp. 1661-1681
    • Dunbrack R.L., Jr.1    Cohen, F.E.2
  • 16
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox, K.M., Dias, J.A. and Van Roey, P. (2001) Three-dimensional structure of human follicle-stimulating hormone. Mol. Endocrinol., 15, 378-389.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 17
    • 0030969880 scopus 로고    scopus 로고
    • Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH
    • Grossmann, M., Szkudlinski, M.W., Wong, R., Dias, J.A., Ji, T.H. and Weintraub, B.D. (1997) Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH. J. Biol. Chem., 272, 15532-15540.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15532-15540
    • Grossmann, M.1    Szkudlinski, M.W.2    Wong, R.3    Dias, J.A.4    Ji, T.H.5    Weintraub, B.D.6
  • 18
    • 0029646089 scopus 로고
    • Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions
    • Jiang, X., Dreano, M., Buckler, D.R., Cheng, S., Ythier, A., Wu, H., Hendrickson, W.A. and el Tayar, N. (1995) Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure, 3, 1341-1353.
    • (1995) Structure , vol.3 , pp. 1341-1353
    • Jiang, X.1    Dreano, M.2    Buckler, D.R.3    Cheng, S.4    Ythier, A.5    Wu, H.6    Hendrickson, W.A.7    El Tayar, N.8
  • 19
    • 0036232188 scopus 로고    scopus 로고
    • Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information
    • Kajava, A.V. and Kobe, B. (2002) Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information. Protein Sci., 11, 1082-1090.
    • (2002) Protein Sci. , vol.11 , pp. 1082-1090
    • Kajava, A.V.1    Kobe, B.2
  • 20
    • 0029645408 scopus 로고
    • Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats
    • Kajava, A.V., Vassart, G. and Wodak, S.J. (1995) Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure, 3, 867-877.
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 21
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe, B. and Deisenhofer, J. (1993) Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature, 366, 751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 22
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe, B. and Deisenhofer, J. (1995) A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature, 374, 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 23
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B. and Kajava, A.V. (2001) The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol., 11, 725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 945-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 945-950
    • Kraulis, P.J.1
  • 26
    • 0031889436 scopus 로고    scopus 로고
    • A comprehensive evolutionary analysis based on nucleoticle and amino acid sequences of the α- and β-subunits of glycoprotein hormone gene family
    • Li, M.D. and Ford, J.J. (1998) A comprehensive evolutionary analysis based on nucleoticle and amino acid sequences of the α- and β-subunits of glycoprotein hormone gene family. J. Endocrinol., 156, 529-542.
    • (1998) J. Endocrinol. , vol.156 , pp. 529-542
    • Li, M.D.1    Ford, J.J.2
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. (1997) Raster3D: photorealistic molecular graphics. Methods Enzymol., 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 30
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle, W.R., Campbell, R.K., Rao, S.N., Ayad, N.G., Bernard, M.P., Han, Y. and Wang, Y. (1995) Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J. Biol. Chem., 270, 20020-20031.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20020-20031
    • Moyle, W.R.1    Campbell, R.K.2    Rao, S.N.3    Ayad, N.G.4    Bernard, M.P.5    Han, Y.6    Wang, Y.7
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 32
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatam, T.E., DeBolt, S., Ferguson, D.M., Seibel, G. and Kollman, P.A. (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun., 91, 1-41.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatam, T.E.5    DeBolt, S.6    Ferguson, D.M.7    Seibel, G.8    Kollman, P.A.9
  • 34
    • 0035910404 scopus 로고    scopus 로고
    • Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex
    • Remy, J.J., Nespoulous, C., Grosclaude, J., Grebert, D., Couture, L., Pajot, E. and Salesse, R. (2001) Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex. J. Biol. Chem., 276, 1681-1687.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1681-1687
    • Remy, J.J.1    Nespoulous, C.2    Grosclaude, J.3    Grebert, D.4    Couture, L.5    Pajot, E.6    Salesse, R.7
  • 35
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equation of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.P., Ciccotti, G. and Berendsen, H. (1977) Numerical integration of the cartesian equation of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys., 00, 327-341.
    • (1977) J. Comput. Phys. , vol.0 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.3
  • 36
    • 0037033014 scopus 로고    scopus 로고
    • Structural requirements for mutational lutropin/choriogonadotropin receptor activation
    • Sangkuhl, K., Schulz, A., Schultz, G. and Schoneberg, T. (2002) Structural requirements for mutational lutropin/choriogonadotropin receptor activation. J. Biol. Chem., 277, 47748-47755.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47748-47755
    • Sangkuhl, K.1    Schulz, A.2    Schultz, G.3    Schoneberg, T.4
  • 37
    • 0033031526 scopus 로고    scopus 로고
    • Clinical aspects of ovarian hyperstimulation syndrome
    • Schenker, J.G. (1999) Clinical aspects of ovarian hyperstimulation syndrome. Eur. J. Obstet. Gynecol. Reprod. Biol., 85, 13-20.
    • (1999) Eur. J. Obstet. Gynecol. Reprod. Biol. , vol.85 , pp. 13-20
    • Schenker, J.G.1
  • 38
    • 0035968185 scopus 로고    scopus 로고
    • Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin
    • Schmidt, A., MacColl, R., Lindau-Shepard,B., Buckler, D.R. and Dias, J.A. (2001) Hormone-induced conformational change of the purified soluble hormone binding domain of follitropin receptor complexed with single chain follitropin. J. Biol. Chem., 276, 23373-23381.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23373-23381
    • Schmidt, A.1    MacColl, R.2    Lindau-Shepard, B.3    Buckler, D.R.4    Dias, J.A.5
  • 39
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber, G. (2002) Kinetic studies of protein-protein interactions. Curr. Opin. Struct. Biol., 12, 41-47.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 40
    • 0037225463 scopus 로고    scopus 로고
    • Specificity of cognate ligand-receptor interactions: Fusion proteins of human chorionic gonadotropin and the heptahelical receptors for human luteinizing hormone, thyroid-stimulating hormone and follicle-stimulating hormone
    • Schubert, R.L., Narayan, P. and Puett, D. (2003) Specificity of cognate ligand-receptor interactions: fusion proteins of human chorionic gonadotropin and the heptahelical receptors for human luteinizing hormone, thyroid-stimulating hormone and follicle-stimulating hormone. Endocrinology, 144, 129-137.
    • (2003) Endocrinology , vol.144 , pp. 129-137
    • Schubert, R.L.1    Narayan, P.2    Puett, D.3
  • 41
    • 0036218255 scopus 로고    scopus 로고
    • Lysine 183 and glutamic acid 157 of the TSH receptor: Two interacting residues with a key role in determining specificity toward TSH and human CG
    • Smits, G., Govaerts, C., Nubourgh, I., Pardo, L., Vassart, G. and Costagliola, S. (2002) Lysine 183 and glutamic acid 157 of the TSH receptor: two interacting residues with a key role in determining specificity toward TSH and human CG. Mol. Endocrinol., 16, 722-735.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 722-735
    • Smits, G.1    Govaerts, C.2    Nubourgh, I.3    Pardo, L.4    Vassart, G.5    Costagliola, S.6
  • 43
    • 0036083401 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski, M.W., Fremont, V., Ronin, C. and Weintraub, B.D. (2002) Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships. Physiol. Rev., 82, 473-502.
    • (2002) Physiol. Rev. , vol.82 , pp. 473-502
    • Szkudlinski, M.W.1    Fremont, V.2    Ronin, C.3    Weintraub, B.D.4
  • 44
    • 0036214718 scopus 로고    scopus 로고
    • Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist
    • Vlaeminck-Guillem, V., Ho, S.C., Rodien, P., Vassart, G. and Costagliola, S. (2002) Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist. Mol. Endocrinol., 16, 736-746.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 736-746
    • Vlaeminck-Guillem, V.1    Ho, S.C.2    Rodien, P.3    Vassart, G.4    Costagliola, S.5
  • 45
    • 0034704346 scopus 로고    scopus 로고
    • Bifunctional hCG analogs adopt different conformations in LH and FSH receptor complexes
    • Wang, Y., Bernard, M.P. and Moyle, W.R. (2000) Bifunctional hCG analogs adopt different conformations in LH and FSH receptor complexes. Mol. Cell. Endocrinol., 170, 67-77.
    • (2000) Mol. Cell. Endocrinol. , vol.170 , pp. 67-77
    • Wang, Y.1    Bernard, M.P.2    Moyle, W.R.3
  • 46
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J.W., Liu, Y., Canfield, R.E. and Hendrickson, W.A. (1994) Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. Structure, 2, 545-558.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.