메뉴 건너뛰기




Volumn 113, Issue 2, 2007, Pages 410-419

Thyrotropin-releasing hormone and its receptors - A hypothesis for binding and receptor activation

Author keywords

Active conformation; Agonist; GPCR activation; Ligand binding; Structure activity relationships; TRH receptor

Indexed keywords

CELL SURFACE RECEPTOR; G PROTEIN COUPLED RECEPTOR; PROTIRELIN; PROTIRELIN RECEPTOR;

EID: 33846428430     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2006.09.004     Document Type: Review
Times cited : (33)

References (41)
  • 1
    • 0033735198 scopus 로고    scopus 로고
    • Juxtamembrane regions in the third intracellular loop of the thyrotropin-releasing hormone receptor type 1 are important for coupling to Gq
    • Buck F., Wang W., Harder S., Brathwaite C., Bruhn T.O., and Gershengorn M.C. Juxtamembrane regions in the third intracellular loop of the thyrotropin-releasing hormone receptor type 1 are important for coupling to Gq. Endocrinology 141 (2000) 3717-3722
    • (2000) Endocrinology , vol.141 , pp. 3717-3722
    • Buck, F.1    Wang, W.2    Harder, S.3    Brathwaite, C.4    Bruhn, T.O.5    Gershengorn, M.C.6
  • 2
    • 0032212497 scopus 로고    scopus 로고
    • Thyrotropin releasing hormone analogs: A building block approach to the construction of tetracyclic peptidomimetics
    • Chu W., Perlman J.H., Gershengorn M.C., and Moeller K.D. Thyrotropin releasing hormone analogs: A building block approach to the construction of tetracyclic peptidomimetics. Bioorg Med Chem Lett 8 (1998) 3093-3096
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 3093-3096
    • Chu, W.1    Perlman, J.H.2    Gershengorn, M.C.3    Moeller, K.D.4
  • 3
    • 0032407855 scopus 로고    scopus 로고
    • A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation
    • Colson A.O., Perlman J.H., Jinsi-Parimoo A., Nussenzveig D.R., Osman R., and Gershengorn M.C. A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation. Mol Pharmacol 54 (1998) 968-978
    • (1998) Mol Pharmacol , vol.54 , pp. 968-978
    • Colson, A.O.1    Perlman, J.H.2    Jinsi-Parimoo, A.3    Nussenzveig, D.R.4    Osman, R.5    Gershengorn, M.C.6
  • 4
    • 0031909269 scopus 로고    scopus 로고
    • Static and dynamic roles of extracellular loops in G-protein-coupled receptors: a mechanism for sequential binding of thyrotropin-releasing hormone to its receptor
    • Colson A.O., Perlman J.H., Smolyar A., Gershengorn M.C., and Osman R. Static and dynamic roles of extracellular loops in G-protein-coupled receptors: a mechanism for sequential binding of thyrotropin-releasing hormone to its receptor. Biophys J 74 (1998) 1087-1100
    • (1998) Biophys J , vol.74 , pp. 1087-1100
    • Colson, A.O.1    Perlman, J.H.2    Smolyar, A.3    Gershengorn, M.C.4    Osman, R.5
  • 5
    • 0015608418 scopus 로고
    • Carbon-13 nuclear magnetic resonance studies on thyrotropin-releasing factor and related peptides
    • Deslauriers R., Garrigou-Lagrange C., Bellocq A.M., and Smith I.C.P. Carbon-13 nuclear magnetic resonance studies on thyrotropin-releasing factor and related peptides. FEBS Lett 31 (1973) 59-66
    • (1973) FEBS Lett , vol.31 , pp. 59-66
    • Deslauriers, R.1    Garrigou-Lagrange, C.2    Bellocq, A.M.3    Smith, I.C.P.4
  • 7
    • 0023173659 scopus 로고
    • Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core
    • Dixon R.A., Sigal I.S., Rands E., Register R.B., Candelore M.R., Blake A.D., et al. Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core. Nature 326 (1987) 73-77
    • (1987) Nature , vol.326 , pp. 73-77
    • Dixon, R.A.1    Sigal, I.S.2    Rands, E.3    Register, R.B.4    Candelore, M.R.5    Blake, A.D.6
  • 8
    • 33744965195 scopus 로고    scopus 로고
    • Low affinity analogs of thyrotropin-releasing hormone are super-agonists
    • Engel S., Neumann S., Kaur N., Monga V., Jain R., Northup J., et al. Low affinity analogs of thyrotropin-releasing hormone are super-agonists. J Biol Chem 281 (2006) 13103-13109
    • (2006) J Biol Chem , vol.281 , pp. 13103-13109
    • Engel, S.1    Neumann, S.2    Kaur, N.3    Monga, V.4    Jain, R.5    Northup, J.6
  • 9
    • 0035117505 scopus 로고    scopus 로고
    • Minireview: insights into G protein-coupled receptor function using molecular models
    • Gershengorn M.C., and Osman R. Minireview: insights into G protein-coupled receptor function using molecular models. Endocrinology 142 (2001) 2-10
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.C.1    Osman, R.2
  • 10
    • 0028838459 scopus 로고
    • Identification of Asn289 as a ligand binding site in the rat thyrotropin-releasing hormone (THR) receptor as determined by complementary modifications in the ligand and receptor: a new model for THR binding
    • Han B., and Tashjian Jr. A.H. Identification of Asn289 as a ligand binding site in the rat thyrotropin-releasing hormone (THR) receptor as determined by complementary modifications in the ligand and receptor: a new model for THR binding. Biochemistry 34 (1995) 13412-13422
    • (1995) Biochemistry , vol.34 , pp. 13412-13422
    • Han, B.1    Tashjian Jr., A.H.2
  • 11
    • 0028786915 scopus 로고
    • Importance of extracellular domains for ligand binding in the thyrotropin-releasing hormone receptor
    • Han B., and Tashjian Jr. A.H. Importance of extracellular domains for ligand binding in the thyrotropin-releasing hormone receptor. Mol Pharmacol 9 (1995) 1708-1719
    • (1995) Mol Pharmacol , vol.9 , pp. 1708-1719
    • Han, B.1    Tashjian Jr., A.H.2
  • 12
    • 0020320407 scopus 로고
    • Rapid temperature-dependent transformation of the thyrotropin-releasing hormone-receptor complex in rat pituitary tumor cells
    • Hinkle P.M., and Kinsella P.A. Rapid temperature-dependent transformation of the thyrotropin-releasing hormone-receptor complex in rat pituitary tumor cells. J Biol Chem 257 (1982) 5462-5470
    • (1982) J Biol Chem , vol.257 , pp. 5462-5470
    • Hinkle, P.M.1    Kinsella, P.A.2
  • 13
    • 14044251558 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches
    • Huang W., Osman R., and Gershengorn M.C. Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches. Biochemistry 44 (2005) 2419-2431
    • (2005) Biochemistry , vol.44 , pp. 2419-2431
    • Huang, W.1    Osman, R.2    Gershengorn, M.C.3
  • 14
    • 9644290890 scopus 로고    scopus 로고
    • Similar dynamics of G-protein coupled receptors molecules in response to antagonist binding
    • Jarv J., and Oras A. Similar dynamics of G-protein coupled receptors molecules in response to antagonist binding. Neurosci Lett 373 (2005) 150-152
    • (2005) Neurosci Lett , vol.373 , pp. 150-152
    • Jarv, J.1    Oras, A.2
  • 16
    • 0029894316 scopus 로고    scopus 로고
    • Restricted analogues provide evidence of a biologically active conformation of thyrotropin-releasing hormone
    • Laakkonen L., Li W., Perlman J.H., Guarnieri F., Osman R., Moeller K.D., et al. Restricted analogues provide evidence of a biologically active conformation of thyrotropin-releasing hormone. Mol Pharmacol 49 (1996) 1092-1096
    • (1996) Mol Pharmacol , vol.49 , pp. 1092-1096
    • Laakkonen, L.1    Li, W.2    Perlman, J.H.3    Guarnieri, F.4    Osman, R.5    Moeller, K.D.6
  • 17
    • 0029894113 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Novel mixed mode Monte Carlo/stochastic dynamics simulations of the complex between TRH and TRH receptor
    • Laakkonen L.J., Guarnieri F., Perlman J.H., Gershengorn M.C., and Osman R. A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Novel mixed mode Monte Carlo/stochastic dynamics simulations of the complex between TRH and TRH receptor. Biochemistry 35 (1996) 7651-7663
    • (1996) Biochemistry , vol.35 , pp. 7651-7663
    • Laakkonen, L.J.1    Guarnieri, F.2    Perlman, J.H.3    Gershengorn, M.C.4    Osman, R.5
  • 18
    • 2142703828 scopus 로고    scopus 로고
    • Synergistic contributions of the functional groups of epinephrine to its affinity and efficacy at the beta2 adrenergic receptor
    • Liapakis G., Chan W.C., Papadokostaki M., and Javitch J.A. Synergistic contributions of the functional groups of epinephrine to its affinity and efficacy at the beta2 adrenergic receptor. Mol Pharmacol 65 (2004) 1181-1190
    • (2004) Mol Pharmacol , vol.65 , pp. 1181-1190
    • Liapakis, G.1    Chan, W.C.2    Papadokostaki, M.3    Javitch, J.A.4
  • 19
    • 6944221315 scopus 로고    scopus 로고
    • A model of inverse agonist action at thyrotropin-releasing hormone receptor type 1: role of a conserved tryptophan in helix 6
    • Lu X., Huang W., Worthington S., Drabik P., Osman R., and Gershengorn M.C. A model of inverse agonist action at thyrotropin-releasing hormone receptor type 1: role of a conserved tryptophan in helix 6. Mol Pharmacol 66 (2004) 1192-1200
    • (2004) Mol Pharmacol , vol.66 , pp. 1192-1200
    • Lu, X.1    Huang, W.2    Worthington, S.3    Drabik, P.4    Osman, R.5    Gershengorn, M.C.6
  • 20
    • 33846409380 scopus 로고    scopus 로고
    • MacroModel (2003). (Version 9.1) [Computer software]. Schrodinger, LLC.: New York, NY, USA.
  • 21
    • 0027448975 scopus 로고
    • Decreased levels of internalized thyrotropin-releasing hormone receptors after uncoupling from guanine nucleotide-binding protein and phospholipase-C
    • Nussenzveig D.R., Heinflink M., and Gershengorn M.C. Decreased levels of internalized thyrotropin-releasing hormone receptors after uncoupling from guanine nucleotide-binding protein and phospholipase-C. Mol Endocrinol 7 (1993) 1105-1111
    • (1993) Mol Endocrinol , vol.7 , pp. 1105-1111
    • Nussenzveig, D.R.1    Heinflink, M.2    Gershengorn, M.C.3
  • 22
    • 0035860802 scopus 로고    scopus 로고
    • The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states
    • Palanche T., Ilien B., Zoffmann S., Reck M.P., Bucher B., Edelstein S.J., et al. The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. J Biol Chem 276 (2001) 34853-34861
    • (2001) J Biol Chem , vol.276 , pp. 34853-34861
    • Palanche, T.1    Ilien, B.2    Zoffmann, S.3    Reck, M.P.4    Bucher, B.5    Edelstein, S.J.6
  • 24
    • 0031444103 scopus 로고    scopus 로고
    • Role of the extracellular loops of the thyrotropin-releasing hormone receptor: evidence for an initial interaction with thyrotropin-releasing hormone
    • Perlman J.H., Colson A.O., Jain R., Czyzewski B., Cohen L.A., and Osman R. Role of the extracellular loops of the thyrotropin-releasing hormone receptor: evidence for an initial interaction with thyrotropin-releasing hormone. Biochemistry 36 (1997) 15670-15676
    • (1997) Biochemistry , vol.36 , pp. 15670-15676
    • Perlman, J.H.1    Colson, A.O.2    Jain, R.3    Czyzewski, B.4    Cohen, L.A.5    Osman, R.6
  • 25
    • 0028908506 scopus 로고
    • Distinct roles for arginines in transmembrane helices 6 and 7 of the thyrotropin-releasing hormone receptor
    • Perlman J.H., Laakkonen L., Osman R., and Gershengorn M.C. Distinct roles for arginines in transmembrane helices 6 and 7 of the thyrotropin-releasing hormone receptor. Mol Pharmacol 47 (1995) 480-484
    • (1995) Mol Pharmacol , vol.47 , pp. 480-484
    • Perlman, J.H.1    Laakkonen, L.2    Osman, R.3    Gershengorn, M.C.4
  • 26
    • 0029953735 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor
    • Perlman J.H., Laakkonen L.J., Guarnieri F., Osman R., and Gershengorn M.C. A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor. Biochemistry 35 (1996) 7643-7650
    • (1996) Biochemistry , vol.35 , pp. 7643-7650
    • Perlman, J.H.1    Laakkonen, L.J.2    Guarnieri, F.3    Osman, R.4    Gershengorn, M.C.5
  • 27
    • 0026496893 scopus 로고
    • Thyrotropin-releasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral peptide binding to G protein-coupled receptors
    • Perlman J.H., Nussenzveig D.R., Osman R., and Gershengorn M.C. Thyrotropin-releasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral peptide binding to G protein-coupled receptors. J Biol Chem 267 (1992) 24413-24417
    • (1992) J Biol Chem , vol.267 , pp. 24413-24417
    • Perlman, J.H.1    Nussenzveig, D.R.2    Osman, R.3    Gershengorn, M.C.4
  • 28
    • 0027989823 scopus 로고
    • A model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Evidence for a second direct interaction between transmembrane helix 3 and TRH
    • Perlman J.H., Laakkonen L., Osman R., and Gershengorn M.C. A model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Evidence for a second direct interaction between transmembrane helix 3 and TRH. J Biol Chem 269 (1994) 23383-23386
    • (1994) J Biol Chem , vol.269 , pp. 23383-23386
    • Perlman, J.H.1    Laakkonen, L.2    Osman, R.3    Gershengorn, M.C.4
  • 29
    • 0028045051 scopus 로고
    • Hydrogen bonding interaction of thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRH receptor
    • Perlman J.H., Thaw C.N., Laakkonen L., Bowers C.Y., Osman R., and Gershengorn M.C. Hydrogen bonding interaction of thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRH receptor. J Biol Chem 269 (1994) 1610-1613
    • (1994) J Biol Chem , vol.269 , pp. 1610-1613
    • Perlman, J.H.1    Thaw, C.N.2    Laakkonen, L.3    Bowers, C.Y.4    Osman, R.5    Gershengorn, M.C.6
  • 30
    • 0028296886 scopus 로고
    • A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation
    • Phillips W.J., and Cerione R.A. A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation. Biochem J 299 Pt 2 (1994) 351-357
    • (1994) Biochem J , vol.299 , Issue.PART 2 , pp. 351-357
    • Phillips, W.J.1    Cerione, R.A.2
  • 31
    • 0015341526 scopus 로고    scopus 로고
    • Synthetic thyrotropin-releasing factor analogs. 3. Effect of replacement or modification of histidine residue on biological activity
    • Rivier J., Vale W., Monahan M., Ling N., and Burgus R. Synthetic thyrotropin-releasing factor analogs. 3. Effect of replacement or modification of histidine residue on biological activity. J Med Chem 15 (2005) 479-4
    • (2005) J Med Chem , vol.15 , pp. 479-4
    • Rivier, J.1    Vale, W.2    Monahan, M.3    Ling, N.4    Burgus, R.5
  • 32
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P., Cotecchia S., Costa T., and Lefkowitz R.J. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 268 (1993) 4625-4636
    • (1993) J Biol Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 34
    • 21844469248 scopus 로고    scopus 로고
    • Rhodopsin: a structural primer for G-protein coupled receptors
    • Stenkamp R.E., Teller D.C., and Palczewski K. Rhodopsin: a structural primer for G-protein coupled receptors. Arch Pharm (Weinheim) 338 (2005) 209-216
    • (2005) Arch Pharm (Weinheim) , vol.338 , pp. 209-216
    • Stenkamp, R.E.1    Teller, D.C.2    Palczewski, K.3
  • 35
    • 0038025925 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone receptors-similarities and differences
    • Sun Y., Lu X., and Gershengorn M.C. Thyrotropin-releasing hormone receptors-similarities and differences. J Mol Endocrinol 30 (2003) 87-97
    • (2003) J Mol Endocrinol , vol.30 , pp. 87-97
    • Sun, Y.1    Lu, X.2    Gershengorn, M.C.3
  • 36
    • 30144441512 scopus 로고    scopus 로고
    • A chemogenomic analysis of the transmembrane binding cavity of human G-protein-coupled receptors
    • Surgand J.S., Rodrigo J., Kellenberger E., and Rognan D. A chemogenomic analysis of the transmembrane binding cavity of human G-protein-coupled receptors. Proteins 62 (2006) 509-538
    • (2006) Proteins , vol.62 , pp. 509-538
    • Surgand, J.S.1    Rodrigo, J.2    Kellenberger, E.3    Rognan, D.4
  • 37
    • 0345791508 scopus 로고    scopus 로고
    • Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states
    • Swaminath G., Xiang Y., Lee T.W., Steenhuis J., Parnot C., and Kobilka B.K. Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states. J Biol Chem 279 (2004) 686-691
    • (2004) J Biol Chem , vol.279 , pp. 686-691
    • Swaminath, G.1    Xiang, Y.2    Lee, T.W.3    Steenhuis, J.4    Parnot, C.5    Kobilka, B.K.6
  • 39
    • 13444261019 scopus 로고    scopus 로고
    • G protein-coupled receptors: a count of 1001 conformations
    • Vauquelin G., and Van I L. G protein-coupled receptors: a count of 1001 conformations. Fundam Clin Pharmacol 19 (2005) 45-56
    • (2005) Fundam Clin Pharmacol , vol.19 , pp. 45-56
    • Vauquelin, G.1    Van I, L.2
  • 41
    • 0037419780 scopus 로고    scopus 로고
    • Impact of Azaproline on Amide Cis-Trans Isomerism: Conformational Analyses and NMR Studies of Model Peptides Including TRH Analogues
    • Zhang W.J., Berglund A., Kao J.L.F., Couty J.P., Gershengorn M.C., and Marshall G.R. Impact of Azaproline on Amide Cis-Trans Isomerism: Conformational Analyses and NMR Studies of Model Peptides Including TRH Analogues. J Am Chem Soc 125 (2003) 1221-1235
    • (2003) J Am Chem Soc , vol.125 , pp. 1221-1235
    • Zhang, W.J.1    Berglund, A.2    Kao, J.L.F.3    Couty, J.P.4    Gershengorn, M.C.5    Marshall, G.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.