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Volumn 5, Issue 5, 1998, Pages 241-254

Functional homodimeric glycoprotein hormones: Implications for hormone action and evolution

Author keywords

Cysteine knot proteins; Evolution; Glycoprotein hormone evolution; Glycoprotein hormones; Lutropin receptors; Protein minimization

Indexed keywords


EID: 0032078255     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90617-2     Document Type: Article
Times cited : (27)

References (41)
  • 1
    • 0028239813 scopus 로고
    • Crystal structure of human chorionic gonadotropin
    • Lapthorn, A.J. et al., & Isaacs, N.W. (1994). Crystal structure of human chorionic gonadotropin. Nature 369, 455-461.
    • (1994) Nature , vol.369 , pp. 455-461
    • Lapthorn, A.J.1    Isaacs, N.W.2
  • 2
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J.W., Liu, Y., Canfield, R.E. & Hendrickspn, W.A. (1994). Structure of human chorionic gonadotropin at 2.6 Å 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    Hendrickspn, W.A.5
  • 3
    • 0019831147 scopus 로고
    • The gene encoding the common alpha subunit of the four human glycoprotein hormones
    • Fiddes, J.C. & Goodman, H.M. (1981). The gene encoding the common alpha subunit of the four human glycoprotein hormones. J. Mol. Appl. Genet. 1, 3-18.
    • (1981) J. Mol. Appl. Genet. , vol.1 , pp. 3-18
    • Fiddes, J.C.1    Goodman, H.M.2
  • 4
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce, J.G. & Parsons, T.F. (1981). Glycoprotein hormones: structure and function. Annu. Rev. Biochem. 50, 465-495.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 5
    • 0026081701 scopus 로고
    • Conversion of human choriogonadotropin into a follitropin by protein engineering
    • Campbell, R.K., Dean Emig, D.M. & Moyle, W.R. (1991). Conversion of human choriogonadotropin into a follitropin by protein engineering. Proc. Natl Acad. Sci. USA 88, 760-764.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 760-764
    • Campbell, R.K.1    Dean Emig, D.M.2    Moyle, W.R.3
  • 7
    • 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. & 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
  • 8
    • 0030969880 scopus 로고    scopus 로고
    • Substitution of the seatbelt region of the thyroid stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers lutropin but not follitropin activity to chimeric TSH
    • Grossman, M., Szkudlinski, M.W., Wong, R., Dias, J.A., Ji, T.H. & Weintraub, B.D. (1997). Substitution of the seatbelt region of the thyroid stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers lutropin but not follitropin activity to chimeric TSH. J. Biol. Chem. 272, 15532-15540.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15532-15540
    • Grossman, M.1    Szkudlinski, M.W.2    Wong, R.3    Dias, J.A.4    Ji, T.H.5    Weintraub, B.D.6
  • 9
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin (hCG) and lutropin receptor (LHR) interaction that explains signal transduction of the glycoprotein hormones
    • Moyle, W.R. et al., & Wang, X. (1995). Model of human chorionic gonadotropin (hCG) and lutropin receptor (LHR) 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    Wang, X.2
  • 10
    • 0029646089 scopus 로고
    • Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions
    • Jiang, X. et al. & el Tayer, 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    El Tayer, N.2
  • 11
    • 0024813415 scopus 로고
    • Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β-subunit
    • Suganuma, N., Matzuk, M.M. & Boime, I. (1990). Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β-subunit. J. Biol. Chem. 264, 19302-19307.
    • (1990) J. Biol. Chem. , vol.264 , pp. 19302-19307
    • Suganuma, N.1    Matzuk, M.M.2    Boime, I.3
  • 12
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S. & Alber, T. (1991). X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil. Science 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 13
    • 0030606149 scopus 로고    scopus 로고
    • hCGβ residues 94-96 alter LH activity without appearing to make key receptor contacts
    • Han, Y., Bernard, M.P. & Moyle, W.R. (1996). hCGβ residues 94-96 alter LH activity without appearing to make key receptor contacts. Mol. Cell. Endocrinol. 124, 151-161.
    • (1996) Mol. Cell. Endocrinol. , vol.124 , pp. 151-161
    • Han, Y.1    Bernard, M.P.2    Moyle, W.R.3
  • 14
    • 0025309387 scopus 로고
    • Localization of residues that confer antibody binding specificity using human chorionic gonadotropin/luteinizing hormone beta subunit chimeras and mutants
    • Moyle, W.R. et al., & Boime, I. (1990). Localization of residues that confer antibody binding specificity using human chorionic gonadotropin/luteinizing hormone beta subunit chimeras and mutants. J. Biol. Chem. 265, 8511-8518.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8511-8518
    • Moyle, W.R.1    Boime, I.2
  • 15
    • 0001653033 scopus 로고
    • Use of monoclonal antibodies to hCG subunits to examine the orientation of hCG in the hormone-receptor complex
    • Moyle, W.R., Ehrlich, P.H. & Canfield, R.E. (1982). Use of monoclonal antibodies to hCG subunits to examine the orientation of hCG in the hormone-receptor complex. Proc. Natl Acad. Sci. USA 79, 2245-2249.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 2245-2249
    • Moyle, W.R.1    Ehrlich, P.H.2    Canfield, R.E.3
  • 16
    • 0029125838 scopus 로고
    • The groove between the α- and β-subunits of hormones with lutropin (LH) activity appears to contact the LH receptor and its conformation is changed during hormone binding
    • Cosowsky, L., Rao, S.N.V., Macdonald, G.J., Papkoff, H., Campbell, R.K. & Moyle, W.R. (1995). The groove between the α- and β-subunits of hormones with lutropin (LH) activity appears to contact the LH receptor and its conformation is changed during hormone binding. J. Biol. Chem. 270, 20011-20019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20011-20019
    • Cosowsky, L.1    Rao, S.N.V.2    Macdonald, G.J.3    Papkoff, H.4    Campbell, R.K.5    Moyle, W.R.6
  • 17
    • 0023941649 scopus 로고
    • The role of the asparagine-linked oligosaccharides of the alpha subunit in the secretion and assembly of human chorionic gonadotrophin
    • Matzuk, M.M. & Boime, I. (1988). The role of the asparagine-linked oligosaccharides of the alpha subunit in the secretion and assembly of human chorionic gonadotrophin. J. Cell. Biol. 106, 1049-1059.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1049-1059
    • Matzuk, M.M.1    Boime, I.2
  • 18
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk, M.M., Keene, J.L. & Boime, I. (1989). Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J. Biol. Chem. 264, 2409-2414.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 19
    • 0026635335 scopus 로고
    • The carboxy-terminal region of the glycoprotein hormone alpha-subunit: Contributions to receptor binding and signaling in human chorionic gonadotropin
    • Chen, F., Wang, Y. & Puett, D. (1992). The carboxy-terminal region of the glycoprotein hormone alpha-subunit: contributions to receptor binding and signaling in human chorionic gonadotropin. Mol. Endocrinol. 6, 914-919.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 914-919
    • Chen, F.1    Wang, Y.2    Puett, D.3
  • 20
    • 0025990729 scopus 로고
    • Conversion of lysine 91 to methionine or glutamic acid in human choriogonadotropin a results in the loss of cAMP inducibility
    • Yoo, J., Ji, I. & Ji, T.H. (1991). Conversion of lysine 91 to methionine or glutamic acid in human choriogonadotropin a results in the loss of cAMP inducibility. J. Biol. Chem. 266, 17741-17743.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17741-17743
    • Yoo, J.1    Ji, I.2    Ji, T.H.3
  • 21
    • 0029824825 scopus 로고    scopus 로고
    • NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit
    • De Beer, T. et al., & Vliegenthart, J.F. (1996). NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. Eur. J. Biochem. 241, 229-242.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 229-242
    • De Beer, T.1    Vliegenthart, J.F.2
  • 22
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A.M., Ultsch, M. & Kossiakoff, A.A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 23
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta
    • Vigers, G.P., Anderson, L.J., Caffes, P. & Brandhuber, B.J. (1997). Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature 386, 190-194.
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 24
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann, C., Fuh, G., Christinger, H.W., Eigenbrot, C., Wells, J.A. & de Vos, A. (1997). Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell 91, 695-704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    De Vos, A.6
  • 25
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller, Y.A., Li, B., Christinger, H.W., Wells, J.A., Cunningham & De, V.A. (1997). Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc. Natl Acad. Sci. USA 94, 7192-7197.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham5    De, V.A.6
  • 26
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. & 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
  • 27
    • 0031032647 scopus 로고    scopus 로고
    • Influence of subunit interactions on lutropin specificity: Implications for studies of glycoprotein hormone function
    • Cosowsky, L., Lin, W., Han, Y., Bernard, M.P., Campbell, R.K. & Moyle, W.R. (1997). Influence of subunit interactions on lutropin specificity: implications for studies of glycoprotein hormone function. J. Biol. Chem. 272, 3309-3314.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3309-3314
    • Cosowsky, L.1    Lin, W.2    Han, Y.3    Bernard, M.P.4    Campbell, R.K.5    Moyle, W.R.6
  • 28
    • 0026042543 scopus 로고
    • Expression of human luteinizing hormone (LH) receptor: Interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species
    • Jia, X.C. et al., & Hsueh, A.J. (1991). Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species. Mol. Endocrinol. 5, 759-768.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 759-768
    • Jia, X.C.1    Hsueh, A.J.2
  • 30
    • 0030985412 scopus 로고    scopus 로고
    • Structural mimicry of a native protein by a minimized binding domain
    • Starovasnik, M.A., Braisted, A.C. & Wells, J.A. (1997). Structural mimicry of a native protein by a minimized binding domain. Proc. Natl Acad. Sci. USA 94, 10080-10085.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10080-10085
    • Starovasnik, M.A.1    Braisted, A.C.2    Wells, J.A.3
  • 31
    • 0030989670 scopus 로고    scopus 로고
    • X-ray structure of glial cell-derived neurotrophic factor at 1.9 a resolution and implications for receptor binding
    • Eigenbrot, C. & Gerber, N. (1997). X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding. Nat. Struct. Biol. 4, 435-438.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 435-438
    • Eigenbrot, C.1    Gerber, N.2
  • 32
    • 0023550308 scopus 로고
    • Detection of conformational changes in human chorionic gonadotropin upon binding to rat gonadal receptors
    • Moyle, W.R. et al., & Erlich, P.H. (1987). Detection of conformational changes in human chorionic gonadotropin upon binding to rat gonadal receptors. J. Biol. Chem. 262, 16920-16926.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16920-16926
    • Moyle, W.R.1    Erlich, P.H.2
  • 33
    • 0026817136 scopus 로고
    • Reconstructing history with amino acid sequences
    • Doolittle, R.F. (1992). Reconstructing history with amino acid sequences. Protein Sci, 191-200.
    • (1992) Protein Sci , pp. 191-200
    • Doolittle, R.F.1
  • 34
    • 0016794917 scopus 로고
    • The molecular evolution of pituitary hormones
    • Wallis, M. (1973). The molecular evolution of pituitary hormones. Biol. Rev. 50, 35-98.
    • (1973) Biol. Rev. , vol.50 , pp. 35-98
    • Wallis, M.1
  • 35
    • 0028942852 scopus 로고
    • Inhibin, activin and the female reproductive axis
    • Woodruff, T.K. & Mather, J.P. (1995). Inhibin, activin and the female reproductive axis. Annu. Rev. Physiol. 57, 219-244.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 219-244
    • Woodruff, T.K.1    Mather, J.P.2
  • 36
    • 0028116115 scopus 로고
    • Mutagenesis of cysteine residues in the human gonadotropin α-subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity
    • Furuhashi, M. et al., & Boime, I. (1994). Mutagenesis of cysteine residues in the human gonadotropin α-subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity. J. Biol. Chem. 269, 25543-25548.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25543-25548
    • Furuhashi, M.1    Boime, I.2
  • 37
    • 0027193414 scopus 로고
    • Amino/carboxyl-terminal deletion mutants of human choriogonadotropin beta
    • Huang, J., Chen, F. & Puett, D. (1993). Amino/carboxyl-terminal deletion mutants of human choriogonadotropin beta. J. Biol. Chem. 268, 9311-9315.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9311-9315
    • Huang, J.1    Chen, F.2    Puett, D.3
  • 38
    • 0028983425 scopus 로고
    • The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity
    • Slaughter, S., Wang, Y.H., Myers, R.V. & Moyle, W.R. (1995). The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity. Mol. Cell. Endocrinol. 112, 21-25.
    • (1995) Mol. Cell. Endocrinol. , vol.112 , pp. 21-25
    • Slaughter, S.1    Wang, Y.H.2    Myers, R.V.3    Moyle, W.R.4
  • 39
    • 0019166519 scopus 로고
    • The cDNA for the β-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3′-untranslated region
    • Fiddes, J.C. & Goodman, H.M. (1980). The cDNA for the β-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3′-untranslated region. Nature 286, 684-687.
    • (1980) Nature , vol.286 , pp. 684-687
    • Fiddes, J.C.1    Goodman, H.M.2
  • 40
    • 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. & 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
  • 41
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kapatein, R. & Thornton, J.M. (1996). AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomolec. NMR 8, 477-486.
    • (1996) J. Biomolec. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kapatein, R.4    Thornton, J.M.5


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