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Volumn 260-262, Issue , 2007, Pages 83-92

Follitropin receptors contain cryptic ligand binding sites

Author keywords

Cryptic ligand binding site; Follitropin; Human choriogonadotropin

Indexed keywords

CHORIONIC GONADOTROPIN; FOLLITROPIN; FOLLITROPIN RECEPTOR; LEUCINE; LIGAND;

EID: 33751242029     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2006.06.012     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0032211789 scopus 로고    scopus 로고
    • Lutropins appear to contact two independent sites in the extracellular domain of their receptors
    • Bernard M.P., Myers R.V., and Moyle W.R. Lutropins appear to contact two independent sites in the extracellular domain of their receptors. Biochem. J. 335 (1998) 611-617
    • (1998) Biochem. J. , vol.335 , pp. 611-617
    • Bernard, M.P.1    Myers, R.V.2    Moyle, W.R.3
  • 2
    • 1642421048 scopus 로고    scopus 로고
    • Tight attachment of chitin binding domain tagged proteins to surfaces coated with acetylated chitosan
    • Bernard M.P., Cao D., Myers R.V., and Moyle W.R. Tight attachment of chitin binding domain tagged proteins to surfaces coated with acetylated chitosan. Anal. Biochem. 327 (2004) 278-283
    • (2004) Anal. Biochem. , vol.327 , pp. 278-283
    • Bernard, M.P.1    Cao, D.2    Myers, R.V.3    Moyle, W.R.4
  • 3
    • 0025847496 scopus 로고
    • Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity
    • Braun T., Schofield P.R., and Sprengel R. Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity. EMBO J. 10 (1991) 1885-1890
    • (1991) EMBO J. , vol.10 , pp. 1885-1890
    • Braun, T.1    Schofield, P.R.2    Sprengel, R.3
  • 5
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger S., Marullo S., and Bouvier M. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26 3 (2005) 131-137
    • (2005) Trends Pharmacol. Sci. , vol.26 , Issue.3 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 7
    • 12744279354 scopus 로고    scopus 로고
    • Endocrinology: fertility hormone in repose
    • Dias J.A. Endocrinology: fertility hormone in repose. Nature 433 7023 (2005) 203-204
    • (2005) Nature , vol.433 , Issue.7023 , pp. 203-204
    • Dias, J.A.1
  • 8
    • 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. 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 (1994) 25289-25294
    • (1994) J. Biol. Chem. , vol.269 , pp. 25289-25294
    • Dias, J.A.1    Zhang, Y.2    Liu, X.3
  • 9
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan Q.R., and Hendrickson W.A. Structure of human follicle-stimulating hormone in complex with its receptor. Nature 433 7023 (2005) 269-277
    • (2005) Nature , vol.433 , Issue.7023 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 10
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox K.M., Dias J.A., and Van Roey P. Three-dimensional structure of human follicle-stimulating hormone. Mol. Endocrinol. 15 (2001) 378-389
    • (2001) Mol. Endocrinol. , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 11
    • 0034456625 scopus 로고    scopus 로고
    • Male hypogonadism caused by homozygous deletion of exon 10 of the luteinizing hormone (LH) receptor: differential action of human chorionic gonadotropin and LH
    • Gromoll J., Eiholzer U., Nieschlag E., and Simoni M. Male hypogonadism caused by homozygous deletion of exon 10 of the luteinizing hormone (LH) receptor: differential action of human chorionic gonadotropin and LH. J. Clin. Endocrinol. Metab. 85 6 (2000) 2281-2286
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , Issue.6 , pp. 2281-2286
    • Gromoll, J.1    Eiholzer, U.2    Nieschlag, E.3    Simoni, M.4
  • 12
    • 0030969880 scopus 로고    scopus 로고
    • Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) beta-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. Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) beta-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH. J. Biol. Chem. 272 24 (1997) 15532-15540
    • (1997) J. Biol. Chem. , vol.272 , Issue.24 , 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
  • 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., and Moyle W.R. hCGβ residues 94-96 alter LH activity without appearing to make key receptor contacts. Mol. Cell. Endocrinol. 124 (1996) 151-161
    • (1996) Mol. Cell. Endocrinol. , vol.124 , pp. 151-161
    • Han, Y.1    Bernard, M.P.2    Moyle, W.R.3
  • 14
    • 6944237210 scopus 로고    scopus 로고
    • The ants go marching two by two: oligomeric structure of G-protein-coupled receptors
    • Javitch J.A. The ants go marching two by two: oligomeric structure of G-protein-coupled receptors. Mol. Pharmacol. 66 5 (2004) 1077-1082
    • (2004) Mol. Pharmacol. , vol.66 , Issue.5 , pp. 1077-1082
    • Javitch, J.A.1
  • 15
    • 85047686522 scopus 로고    scopus 로고
    • Cis- and trans-activation of hormone receptors: the LH receptor
    • Ji I., Lee C., Song Y., Conn P.M., and Ji T.H. Cis- and trans-activation of hormone receptors: the LH receptor. Mol. Endocrinol. 16 6 (2002) 1299-1308
    • (2002) Mol. Endocrinol. , vol.16 , Issue.6 , pp. 1299-1308
    • Ji, I.1    Lee, C.2    Song, Y.3    Conn, P.M.4    Ji, T.H.5
  • 16
    • 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., Tayar N.E., and el Tayar N. Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure 3 12 (1995) 1341-1353
    • (1995) Structure , vol.3 , Issue.12 , 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    Tayar, N.E.8    el Tayar, N.9
  • 18
    • 0034964204 scopus 로고    scopus 로고
    • The GeneMine system for genome/proteome annotation and collaborative data mining
    • Lee C., and Irizarry K. The GeneMine system for genome/proteome annotation and collaborative data mining. IBM Syst. J 40 (2001) 592-603
    • (2001) IBM Syst. J , vol.40 , pp. 592-603
    • Lee, C.1    Irizarry, K.2
  • 19
    • 0033603467 scopus 로고    scopus 로고
    • Addition of an N-terminal dimerization domain promotes assembly of hCG analogs: implications for subunit combination and structure-function analysis
    • Lin W., Ransom M.X., Myers R.V., Bernard M.P., and Moyle W.R. Addition of an N-terminal dimerization domain promotes assembly of hCG analogs: implications for subunit combination and structure-function analysis. Mol. Cell. Endocrinol. 152 (1999) 91-98
    • (1999) Mol. Cell. Endocrinol. , vol.152 , pp. 91-98
    • Lin, W.1    Ransom, M.X.2    Myers, R.V.3    Bernard, M.P.4    Moyle, W.R.5
  • 25
    • 1542330973 scopus 로고    scopus 로고
    • Chorionic gonadotrophin beta subunit mRNA but not luteinising hormone beta subunit mRNA is expressed in the pituitary of the common marmoset (Callithrix jacchus)
    • Muller T., Simoni M., Pekel E., Luetjens C.M., Chandolia R., Amato F., Norman R.J., and Gromoll J. Chorionic gonadotrophin beta subunit mRNA but not luteinising hormone beta subunit mRNA is expressed in the pituitary of the common marmoset (Callithrix jacchus). J. Mol. Endocrinol. 32 1 (2004) 115-128
    • (2004) J. Mol. Endocrinol. , vol.32 , Issue.1 , pp. 115-128
    • Muller, T.1    Simoni, M.2    Pekel, E.3    Luetjens, C.M.4    Chandolia, R.5    Amato, F.6    Norman, R.J.7    Gromoll, J.8
  • 26
    • 0026099739 scopus 로고
    • Equine chorionic gonadotropin
    • Murphy B.D., and Martinuk S.D. Equine chorionic gonadotropin. Endocr. Rev. 12 (1991) 27-44
    • (1991) Endocr. Rev. , vol.12 , pp. 27-44
    • Murphy, B.D.1    Martinuk, S.D.2
  • 28
    • 0034730516 scopus 로고    scopus 로고
    • Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region
    • Nakabayashi K., Kudo M., Kobilka B., and Hsueh A.J. Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region. J. Biol. Chem. 275 (2000) 30264-30271
    • (2000) J. Biol. Chem. , vol.275 , pp. 30264-30271
    • Nakabayashi, K.1    Kudo, M.2    Kobilka, B.3    Hsueh, A.J.4
  • 29
    • 0019729482 scopus 로고
    • Glycoprotein hormones: structure and function.
    • Pierce J.G., and Parsons T.F. Glycoprotein hormones: structure and function. Ann. Rev. Biochem. 50 (1981) 465-495
    • (1981) Ann. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 30
    • 0030913618 scopus 로고    scopus 로고
    • Cloning, sequencing and in vitro functional expression of recombinant donkey follicle-stimulating hormone receptor: a new insight into the binding specificity of gonadotrophin receptors
    • Richard F., Martinat N., Remy J.J., Salesse R., and Combarnous Y. Cloning, sequencing and in vitro functional expression of recombinant donkey follicle-stimulating hormone receptor: a new insight into the binding specificity of gonadotrophin receptors. J. Mol. Endocrinol. 18 3 (1997) 193-202
    • (1997) J. Mol. Endocrinol. , vol.18 , Issue.3 , pp. 193-202
    • Richard, F.1    Martinat, N.2    Remy, J.J.3    Salesse, R.4    Combarnous, Y.5
  • 31
    • 0029092241 scopus 로고
    • Luteinizing hormone/chorionic gonadotropin bioactivity in the common marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule with a structure intermediate between human chorionic gonadotropin and human luteinizing hormone
    • Simula A.P., Amato F., Faast R., Lopata A., Berka J., and Norman. Luteinizing hormone/chorionic gonadotropin bioactivity in the common marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule with a structure intermediate between human chorionic gonadotropin and human luteinizing hormone. Biol. Reprod. 53 2 (1995) 380-389
    • (1995) Biol. Reprod. , vol.53 , Issue.2 , pp. 380-389
    • Simula, A.P.1    Amato, F.2    Faast, R.3    Lopata, A.4    Berka, J.5    Norman6
  • 32
  • 33
    • 0041464853 scopus 로고    scopus 로고
    • Ovarian hyperstimulation syndrome due to a mutation in the follicle-stimulating hormone receptor
    • Smits G., Olatunbosun O., Delbaere A., Pierson R., Vassart G., and Costagliola S. Ovarian hyperstimulation syndrome due to a mutation in the follicle-stimulating hormone receptor. N. Engl. J. Med. 349 8 (2003) 760-766
    • (2003) N. Engl. J. Med. , vol.349 , Issue.8 , pp. 760-766
    • Smits, G.1    Olatunbosun, O.2    Delbaere, A.3    Pierson, R.4    Vassart, G.5    Costagliola, S.6
  • 34
    • 0019989719 scopus 로고
    • Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter
    • Southern P.J., and Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J. Mol. Appl. Genet. 1 4 (1982) 327-341
    • (1982) J. Mol. Appl. Genet. , vol.1 , Issue.4 , pp. 327-341
    • Southern, P.J.1    Berg, P.2
  • 35
    • 1542316313 scopus 로고    scopus 로고
    • A molecular dissection of the glycoprotein hormone receptors
    • Vassart G., Pardo L., and Costagliola S. A molecular dissection of the glycoprotein hormone receptors. TIBS 29 3 (2004) 119-126
    • (2004) TIBS , vol.29 , Issue.3 , pp. 119-126
    • Vassart, G.1    Pardo, L.2    Costagliola, S.3
  • 36
    • 0001442921 scopus 로고
    • Comparative studies of mammalian glycoprotein hormones
    • Alexander N.J. (Ed), Harper and Row, New York
    • Ward D.N., and Moore W.T. Comparative studies of mammalian glycoprotein hormones. In: Alexander N.J. (Ed). Animal Models for Research on Contraception and Fertility (1979), Harper and Row, New York 151-164
    • (1979) Animal Models for Research on Contraception and Fertility , pp. 151-164
    • Ward, D.N.1    Moore, W.T.2
  • 37
    • 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., and Hendrickson W.A. Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2 (1994) 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
  • 38
    • 0035861598 scopus 로고    scopus 로고
    • Alternatively folded choriogonadotropin analogs. Implications for hormone folding and biological activity
    • Xing Y., Lin W., Jiang M., Myers R.V., Cao D., Bernard M.P., and Moyle W.R. Alternatively folded choriogonadotropin analogs. Implications for hormone folding and biological activity. J. Biol. Chem. 276 50 (2001) 46953-46960
    • (2001) J. Biol. Chem. , vol.276 , Issue.50 , pp. 46953-46960
    • Xing, Y.1    Lin, W.2    Jiang, M.3    Myers, R.V.4    Cao, D.5    Bernard, M.P.6    Moyle, W.R.7
  • 39
    • 7244236581 scopus 로고    scopus 로고
    • Use of protein knobs to characterize the position of conserved α-subunit regions in lutropin receptor complexes
    • Xing Y., Lin W., Jiang M., Cao D., Myers R.V., Bernard M.P., and Moyle W.R. Use of protein knobs to characterize the position of conserved α-subunit regions in lutropin receptor complexes. J. Biol. Chem. 279 43 (2004) 44427-44437
    • (2004) J. Biol. Chem. , vol.279 , Issue.43 , pp. 44427-44437
    • Xing, Y.1    Lin, W.2    Jiang, M.3    Cao, D.4    Myers, R.V.5    Bernard, M.P.6    Moyle, W.R.7
  • 40
    • 4143117844 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum. Part IV. Probable mechanism of subunit docking and completion of assembly
    • Xing Y., Myers R.V., Cao D., Lin W., Jiang M., Bernard M.P., and Moyle W.R. Glycoprotein hormone assembly in the endoplasmic reticulum. Part IV. Probable mechanism of subunit docking and completion of assembly. J. Biol. Chem. 279 34 (2004) 35458-35468
    • (2004) J. Biol. Chem. , vol.279 , Issue.34 , pp. 35458-35468
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7


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