메뉴 건너뛰기




Volumn 152, Issue 8, 2011, Pages 3268-3278

Identification of novel TSH interaction sites by systematic binding analysis of the TSHR hinge region

Author keywords

[No Author keywords available]

Indexed keywords

THYROTROPIN; THYROTROPIN RECEPTOR;

EID: 79960729196     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2011-0153     Document Type: Article
Times cited : (9)

References (38)
  • 2
    • 0030985241 scopus 로고    scopus 로고
    • Evidence that the thyrotropin receptor ectodomain contains not one, but two, cleavage sites
    • DOI 10.1210/en.138.7.2893
    • Chazenbalk GD, Tanaka K, Nagayama Y, Kakinuma A, Jaume JC, McLachlan SM, Rapoport B 1997 Evidence that the thyrotropin receptor ectodomain contains not one, but two, cleavage sites. Endocrinology 138:2893-2899 (Pubitemid 27258522)
    • (1997) Endocrinology , vol.138 , Issue.7 , pp. 2893-2899
    • Chazenbalk, G.D.1    Tanaka, K.2    Nagayama, Y.3    Kakinuma, A.4    Jaume, J.C.5    Mclachlan, S.M.6    Rapoport, B.7
  • 3
    • 0025096140 scopus 로고
    • An insertion in the human thyrotropin receptor critical for high affinity hormone binding
    • Wadsworth HL, Chazenbalk GD, Nagayama Y, Russo D, Rapoport B 1990 An insertion in the human thyrotropin receptor critical for high affinity hormone binding. Science 249:1423-1425
    • (1990) Science , vol.249 , pp. 1423-1425
    • Wadsworth, H.L.1    Chazenbalk, G.D.2    Nagayama, Y.3    Russo, D.4    Rapoport, B.5
  • 4
    • 0038182549 scopus 로고    scopus 로고
    • Glycoprotein hormone receptors: Determinants in leucine-rich repeats responsible for ligand specificity
    • DOI 10.1093/emboj/cdg260
    • Smits G, Campillo M, Govaerts C, Janssens V, Richter C, Vassart G, Pardo L, Costagliola S 2003 Glycoprotein hormone receptors: determinants in leucine-rich repeats responsible for ligand specificity. EMBO J 22:2692-2703 (Pubitemid 36712366)
    • (2003) EMBO Journal , vol.22 , Issue.11 , pp. 2692-2703
    • Smits, G.1    Campillo, M.2    Govaerts, C.3    Janssens, V.4    Richter, C.5    Vassart, G.6    Pardo, L.7    Costagliola, S.8
  • 5
    • 78049446704 scopus 로고    scopus 로고
    • Functional differences of invariant and highly conserved residues in the extracellular domain of the glycoprotein hormone receptors
    • Angelova K, de Jonge H, Granneman JC, Puett D, Bogerd J 2010 Functional differences of invariant and highly conserved residues in the extracellular domain of the glycoprotein hormone receptors. J Biol Chem 285:34813-34827
    • (2010) J Biol Chem , vol.285 , pp. 34813-34827
    • Angelova, K.1    De Jonge, H.2    Granneman, J.C.3    Puett, D.4    Bogerd, J.5
  • 6
    • 0037084011 scopus 로고    scopus 로고
    • Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors
    • DOI 10.1093/emboj/21.4.504
    • Costagliola S, Panneels V, Bonomi M, Koch J, Many MC, Smits G, Vassart G 2002 Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. EMBO J 21:504-513 (Pubitemid 34174032)
    • (2002) EMBO Journal , vol.21 , Issue.4 , pp. 504-513
    • Costagliola, S.1    Panneels, V.2    Bonomi, M.3    Koch, J.4    Many, M.C.5    Smits, G.6    Vassart, G.7
  • 7
    • 49649125175 scopus 로고    scopus 로고
    • Extended hormone binding site of the human thyroid stimulating hormone receptor: Distinctive acidic residues in the hinge region are involved in bovine thyroid stimulating hormone binding and receptor activation
    • Mueller S, Kleinau G, Jaeschke H, Paschke R, Krause G 2008 Extended hormone binding site of the human thyroid stimulating hormone receptor: distinctive acidic residues in the hinge region are involved in bovine thyroid stimulating hormone binding and receptor activation. J Biol Chem 283:18048-18055
    • (2008) J Biol Chem , vol.283 , pp. 18048-18055
    • Mueller, S.1    Kleinau, G.2    Jaeschke, H.3    Paschke, R.4    Krause, G.5
  • 8
    • 67650242446 scopus 로고    scopus 로고
    • The superagonistic activity of bovine thyroid-stimulating hormone (TSH) and the human TR1401 TSH analog is determined by specific amino acids in the hinge region of the human TSH receptor
    • Mueller S, Kleinau G, Szkudlinski MW, Jaeschke H, Krause G, Paschke R 2009 The superagonistic activity of bovine thyroid-stimulating hormone (TSH) and the human TR1401 TSH analog is determined by specific amino acids in the hinge region of the human TSH receptor. J Biol Chem 284:16317-16324
    • (2009) J Biol Chem , vol.284 , pp. 16317-16324
    • Mueller, S.1    Kleinau, G.2    Szkudlinski, M.W.3    Jaeschke, H.4    Krause, G.5    Paschke, R.6
  • 9
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan QR, Hendrickson WA 2005 Structure of human follicle-stimulating hormone in complex with its receptor. Nature 433:269-277
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 12
    • 0034282881 scopus 로고    scopus 로고
    • Bioengineering of human thyrotropin superactive analogs by site-directed "lysine-scanning" mutagenesis. Cooperative effects between peripheral loops
    • Leitolf H, Tong KP, Grossmann M, Weintraub BD, Szkudlinski MW 2000 Bioengineering of human thyrotropin superactive analogs by site-directed "lysine-scanning" mutagenesis. Cooperative effects between peripheral loops. J Biol Chem 275:27457-27465
    • (2000) J Biol Chem , vol.275 , pp. 27457-27465
    • Leitolf, H.1    Tong, K.P.2    Grossmann, M.3    Weintraub, B.D.4    Szkudlinski, M.W.5
  • 14
    • 0025989322 scopus 로고
    • The biological activity of bovine and human thyrotropin is differently affected by trypsin treatment of human thyroid cells: Thyroid-stimulating antibody is related to human thyrotropin
    • Foti D, Russo D, Costante G, Filetti S 1991 The biological activity of bovine and human thyrotropin is differently affected by trypsin treatment of human thyroid cells: thyroid-stimulating antibody is related tohumanthyrotropin. J Clin Endocrinol Metab 73:710-716 (Pubitemid 21921928)
    • (1991) Journal of Clinical Endocrinology and Metabolism , vol.73 , Issue.4 , pp. 710-716
    • Foti, D.1    Russo, D.2    Costante, G.3    Filetti, S.4
  • 16
    • 0020418745 scopus 로고
    • Evidence for species specificity in the interaction between thyrotropin and thyroid-stimulating immunoglobulin and their receptor in thyroid tissue
    • Rapoport B, Takai NA, Filetti S 1982 Evidence for species specificity in the interaction between thyrotropin and thyroid-stimulating immunoglobulin and their receptor in thyroid tissue. J Clin Endocrinol Metab 54:1059-1062 (Pubitemid 13243721)
    • (1982) Journal of Clinical Endocrinology and Metabolism , vol.54 , Issue.5 , pp. 1059-1062
    • Rapoport, B.1    Takai, N.A.2    Filetti, S.3
  • 18
    • 0028868298 scopus 로고
    • Potent thyrotropic activity of human chorionic gonadotropin variants in terms of 125I incorporation and de novo synthesized thyroid hormone release inhuman thyroid follicles
    • Yamazaki K, Sato K, Shizume K, Kanaji Y, Ito Y, Obara T, Nakagawa T, Koizumi T, Nishimura R 1995 Potent thyrotropic activity of human chorionic gonadotropin variants in terms of 125I incorporation and de novo synthesized thyroid hormone release inhuman thyroid follicles. J Clin Endocrinol Metab 80:473-479
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 473-479
    • Yamazaki, K.1    Sato, K.2    Shizume, K.3    Kanaji, Y.4    Ito, Y.5    Obara, T.6    Nakagawa, T.7    Koizumi, T.8    Nishimura, R.9
  • 19
    • 2642703472 scopus 로고    scopus 로고
    • Deletions in the third intracellular loop of the thyrotropin receptor. A new mechanism for constitutive activation
    • Wonerow P, Schöneberg T, Schultz G, Gudermann T, Paschke R 1998 Deletions in the third intracellular loop of the thyrotropin receptor. A new mechanism for constitutive activation. J Biol Chem 273:7900-7905
    • (1998) J Biol Chem , vol.273 , pp. 7900-7905
    • Wonerow, P.1    Schöneberg, T.2    Schultz, G.3    Gudermann, T.4    Paschke, R.5
  • 20
    • 0029012098 scopus 로고
    • Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis
    • Swillens S 1995 Interpretation of binding curves obtained with high receptor concentrations: practical aid for computer analysis. Mol Pharmacol 47:1197-1203
    • (1995) Mol Pharmacol , vol.47 , pp. 1197-1203
    • Swillens, S.1
  • 21
    • 33845999291 scopus 로고    scopus 로고
    • Significance of ectodomain cysteine boxes 2 and 3 for the activation mechanism of the thyroid-stimulating hormone receptor
    • DOI 10.1074/jbc.M604770200
    • Mueller S, Kleinau G, Jaeschke H, Neumann S, Krause G, Paschke R 2006 Significance of ectodomain cysteine boxes 2 and 3 for the activation mechanism of the thyroid-stimulating hormone receptor. J Biol Chem 281:31638-31646 (Pubitemid 46041428)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31638-31646
    • Mueller, S.1    Kleinau, G.2    Jaeschke, H.3    Neumann, S.4    Krause, G.5    Paschke, R.6
  • 25
    • 33846631365 scopus 로고    scopus 로고
    • Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource
    • Kleinau G, Brehm M, Wiedemann U, Labudde D, Leser U, Krause G2007 Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource. Mol Endocrinol 21:574-580
    • (2007) Mol Endocrinol , vol.21 , pp. 574-580
    • Kleinau, G.1    Brehm, M.2    Wiedemann, U.3    Labudde, D.4    Leser, U.5    Krause, G.6
  • 26
    • 4344662529 scopus 로고    scopus 로고
    • Minireview: Structural and functional evolution of the thyrotropin receptor
    • DOI 10.1210/en.2004-0437
    • Farid NR, Szkudlinski MW 2004 Minireview: structural and functional evolution of the thyrotropin receptor. Endocrinology 145: 4048-4057 (Pubitemid 39120550)
    • (2004) Endocrinology , vol.145 , Issue.9 , pp. 4048-4057
    • Farid, N.R.1    Szkudlinski, M.W.2
  • 28
    • 0032790015 scopus 로고    scopus 로고
    • An elusive role for glycosylation in the structure and function of reproductive hormones
    • DOI 10.1093/humupd/5.4.330
    • Willey KP 1999 An elusive role for glycosylation in the structure and function of reproductive hormones. Hum Reprod Update 5:330-355 (Pubitemid 29381280)
    • (1999) Human Reproduction Update , vol.5 , Issue.4 , pp. 330-355
    • Willey, K.P.1
  • 29
    • 79952790394 scopus 로고    scopus 로고
    • Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain
    • Chen CR, McLachlan SM, Rapoport B 2011 Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain. J Biol Chem 286:6219-6224
    • (2011) J Biol Chem , vol.286 , pp. 6219-6224
    • Chen, C.R.1    McLachlan, S.M.2    Rapoport, B.3
  • 30
    • 33751530407 scopus 로고    scopus 로고
    • Structural differences in the hinge region of the glycoprotein hormone receptors: Evidence from the sulfated tyrosine residues
    • DOI 10.1210/me.2005-0521
    • Bonomi M, Busnelli M, Persani L, Vassart G, Costagliola S 2006 Structural differences in the hinge region of the glycoprotein hormone receptors: evidence from the sulfated tyrosine residues. Endocrinology 20:3351-3363 (Pubitemid 44833575)
    • (2006) Molecular Endocrinology , vol.20 , Issue.12 , pp. 3351-3363
    • Bonomi, M.1    Busnelli, M.2    Persani, L.3    Vassart, G.4    Costagliola, S.5
  • 31
    • 54449086544 scopus 로고    scopus 로고
    • Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation
    • Bruysters M, Verhoef-Post M, Themmen AP 2008 Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation. J Biol Chem 283:25821-25828
    • (2008) J Biol Chem , vol.283 , pp. 25821-25828
    • Bruysters, M.1    Verhoef-Post, M.2    Themmen, A.P.3
  • 32
    • 43049109876 scopus 로고    scopus 로고
    • The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction
    • DOI 10.1210/me.2007-0407
    • Mizutori Y, Chen CR, McLachlan SM, Rapoport B 2008 The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction. Mol Endocrinol 22:1171-1182 (Pubitemid 351629617)
    • (2008) Molecular Endocrinology , vol.22 , Issue.5 , pp. 1171-1182
    • Mizutori, Y.1    Chen, C.-R.2    McLachlan, S.M.3    Rapoport, B.4
  • 33
    • 78650891915 scopus 로고    scopus 로고
    • Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function
    • Hamidi S, Chen CR, Mizutori-Sasai Y, McLachlan SM, Rapoport B 2011 Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function. Mol Endocrinol 25:184-194
    • (2011) Mol Endocrinol , vol.25 , pp. 184-194
    • Hamidi, S.1    Chen, C.R.2    Mizutori-Sasai, Y.3    McLachlan, S.M.4    Rapoport, B.5
  • 34
    • 0036083401 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski MW, Fremont V, Ronin C, Weintraub BD 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
  • 35
    • 27244435950 scopus 로고    scopus 로고
    • Past, presence and future of thyroid-stimulating hormone (TSH) superactive analogs
    • Szkudlinski MW 2004 Past, presence and future of thyroid-stimulating hormone (TSH) superactive analogs. Cancer Treat Res 122: 345-356
    • (2004) Cancer Treat Res , vol.122 , pp. 345-356
    • Szkudlinski, M.W.1
  • 36
    • 0029883343 scopus 로고    scopus 로고
    • Constitutive activation of the thyrotropin receptor by mutating CYS-636 in the sixth transmembrane segment
    • DOI 10.1006/bbrc.1996.0809
    • Kosugi S, Mori T 1996 Constitutive activation of the thyrotropin receptor by mutating CYS-636 in the sixth transmembrane segment. Biochem Biophys Res Commun 222:713-717 (Pubitemid 26194817)
    • (1996) Biochemical and Biophysical Research Communications , vol.222 , Issue.3 , pp. 713-717
    • Kosugi, S.1    Mori, T.2
  • 37
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • DOI 10.1002/anie.200390319
    • Meyer EA, Castellano RK, Diederich F 2003 Interactions with aromatic rings in chemical and biological recognition. Angew Chem Int Ed Engl 42:1210-1250 (Pubitemid 36410287)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.11 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 38
    • 0027319614 scopus 로고
    • Structure-function studies of the human thyrotropin receptor. Inhibition of binding of labeled thyrotropin (TSH) by synthetic human TSH receptor peptides
    • Morris JC, Bergert ER, McCormick DJ 1993 Structure-function studies of the human thyrotropin receptor. Inhibition of binding of labeled thyrotropin (TSH) by synthetic human TSH receptor peptides. J Biol Chem 268:10900-10905 (Pubitemid 23162271)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.15 , pp. 10900-10905
    • Morris, J.C.1    Bergert, E.R.2    McCormick, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.