메뉴 건너뛰기




Volumn 106, Issue 49, 2009, Pages 20717-20722

Gaining ligand selectivity in thyroid hormone receptors via entropy

Author keywords

Design; Mobility; Triac

Indexed keywords

CARBOXYLIC ACID; CELL NUCLEUS RECEPTOR; THYROID HORMONE RECEPTOR; TIRATRICOL;

EID: 73949144655     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911024106     Document Type: Article
Times cited : (69)

References (40)
  • 1
    • 0034987037 scopus 로고    scopus 로고
    • Selective modulation of thyroid hormone receptor action
    • Baxter JD, et al. (2001) Selective modulation of thyroid hormone receptor action. J Steroid Biochem Mol Biol 76:31-42.
    • (2001) J Steroid Biochem Mol Biol , vol.76 , pp. 31-42
    • Baxter, J.D.1
  • 3
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen PM (2001) Physiological and molecular basis of thyroid hormone action. Physiol Rev 81:1097-1142.
    • (2001) Physiol Rev , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 4
    • 64049099095 scopus 로고    scopus 로고
    • Thyroid hormone mimetics: Potential applications in atherosclerosis, obesity and type 2 diabetes
    • Baxter JD, Webb P (2009) Thyroid hormone mimetics: Potential applications in atherosclerosis, obesity and type 2 diabetes. Nat Rev Drug Discov 8:308-320.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 308-320
    • Baxter, J.D.1    Webb, P.2
  • 5
    • 38649135692 scopus 로고    scopus 로고
    • The thyroid hormone mimetic compound KB2115 lowers plasma LDL cholesterol and stimulates bile acid synthesis without cardiac effects in humans
    • Berkenstam A, et al. (2008) The thyroid hormone mimetic compound KB2115 lowers plasma LDL cholesterol and stimulates bile acid synthesis without cardiac effects in humans. Proc Natl Acad Sci USA 105:663-667.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 663-667
    • Berkenstam, A.1
  • 6
    • 0029643769 scopus 로고
    • Astructural role for hormone in the thyroid hormone receptor
    • Wagner RL, et al. (1995)Astructural role for hormone in the thyroid hormone receptor. Nature 378:690-697.
    • (1995) Nature , vol.378 , pp. 690-697
    • Wagner, R.L.1
  • 7
    • 17744379363 scopus 로고    scopus 로고
    • Hormone selectivity in thyroid hormone receptors
    • Wagner RL, et al. (2001) Hormone selectivity in thyroid hormone receptors. Mol Endocrinol 15:398-410.
    • (2001) Mol Endocrinol , vol.15 , pp. 398-410
    • Wagner, R.L.1
  • 8
    • 0037464499 scopus 로고    scopus 로고
    • Thyroid receptor ligands. 1. Agonist ligands selective for the thyroid receptor β1
    • Ye L, et al. (2003) Thyroid receptor ligands. 1. Agonist ligands selective for the thyroid receptor β1. J Med Chem 46:1580-1588.
    • (2003) J Med Chem , vol.46 , pp. 1580-1588
    • Ye, L.1
  • 9
    • 43049106192 scopus 로고    scopus 로고
    • Structural basis of GC-1 selectivity for thyroid hormone receptor isoforms
    • Bleicher L, et al. (2008) Structural basis of GC-1 selectivity for thyroid hormone receptor isoforms. BMC Struct Biol 8:8.
    • (2008) BMC Struct Biol , vol.8 , pp. 8
    • Bleicher, L.1
  • 10
    • 0347364651 scopus 로고    scopus 로고
    • Ligand selectivity by seeking hydrophobicity in thyroid hormone receptor
    • Borngraeber S, et al. (2003) Ligand selectivity by seeking hydrophobicity in thyroid hormone receptor. Proc Natl Acad Sci USA 100:15358-15363.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15358-15363
    • Borngraeber, S.1
  • 11
    • 0025271659 scopus 로고
    • Binding of 3,5,3′-triiodothyronine (T3) and its analogs to the in vitro translational products of c-erbA protooncogenes: Differences in the affinity of the α- and β-forms for the acetic acid analog and failure of the human testis and kidney α-2 products to bind T3
    • Schueler PA, Schwartz HL, Strait KA, Mariash CN, Oppenheimer JH (1990) Binding of 3,5,3′-triiodothyronine (T3) and its analogs to the in vitro translational products of c-erbA protooncogenes: Differences in the affinity of the α- and β-forms for the acetic acid analog and failure of the human testis and kidney α-2 products to bind T3. Mol Endocrinol 4:227-234.
    • (1990) Mol Endocrinol , vol.4 , pp. 227-234
    • Schueler, P.A.1    Schwartz, H.L.2    Strait, K.A.3    Mariash, C.N.4    Oppenheimer, J.H.5
  • 12
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA (2002) Molecular dynamics simulations of biomolecules. Nat Struct Biol 9:646-652.
    • (2002) Nat Struct Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 13
    • 24144439756 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors
    • Martinez L, et al. (2005) Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors. Biophys J 89:2011-2023.
    • (2005) Biophys J , vol.89 , pp. 2011-2023
    • Martinez, L.1
  • 14
    • 30444446327 scopus 로고    scopus 로고
    • Molecular dynamics simulations of ligand dissociation from thyroid hormone receptors: Evidence of the likeliest escape pathway and its implications for the design of novel ligands
    • Martinez L, Webb P, Polikarpov I, Skaf MS (2006) Molecular dynamics simulations of ligand dissociation from thyroid hormone receptors: Evidence of the likeliest escape pathway and its implications for the design of novel ligands. J Med Chem 49:23-26.
    • (2006) J Med Chem , vol.49 , pp. 23-26
    • Martinez, L.1    Webb, P.2    Polikarpov, I.3    Skaf, M.S.4
  • 15
    • 51849109110 scopus 로고    scopus 로고
    • Only subtle protein conformational adaptations are required for ligand binding to thyroid hormone receptors: Simulations using a novel multipoint steered molecular dynamics approach
    • Martinez L, Polikarpov I, Skaf MS (2008) Only subtle protein conformational adaptations are required for ligand binding to thyroid hormone receptors: Simulations using a novel multipoint steered molecular dynamics approach. J Phys Chem B 112:10741-10751.
    • (2008) J Phys Chem B , vol.112 , pp. 10741-10751
    • Martinez, L.1    Polikarpov, I.2    Skaf, M.S.3
  • 16
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Xiang Z, Soto CS, Honig B (2002) Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction. Proc Natl Acad Sci USA 99:7432-7437.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 17
    • 0030743442 scopus 로고    scopus 로고
    • Augmented hepatic and skeletal thyromimetic effects of tiratricol in comparison with levothyroxine
    • Sherman SI, et al. (1997) Augmented hepatic and skeletal thyromimetic effects of tiratricol in comparison with levothyroxine. J Clin Endocr Metab 82:2153-2158.
    • (1997) J Clin Endocr Metab , vol.82 , pp. 2153-2158
    • Sherman, S.I.1
  • 18
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design
    • Ladbury JE (1996) Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design. Chem Biol 3:973-980.
    • (1996) Chem Biol , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 19
    • 0030758672 scopus 로고    scopus 로고
    • The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: A thermodynamic and crystallography study
    • Holdgate GA, et al. (1997) The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: A thermodynamic and crystallography study. Biochemistry 36:9663-9673.
    • (1997) Biochemistry , vol.36 , pp. 9663-9673
    • Holdgate, G.A.1
  • 20
    • 0033815251 scopus 로고    scopus 로고
    • Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor
    • Velazquez-Campoy A, et al. (2000) Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor. Protein Sci 9:1801-1809.
    • (2000) Protein Sci , vol.9 , pp. 1801-1809
    • Velazquez-Campoy, A.1
  • 21
    • 33646725498 scopus 로고    scopus 로고
    • The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs
    • Kavanagh KL, et al. (2006) The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs. Proc Natl Acad Sci USA 103:7829-7834.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7829-7834
    • Kavanagh, K.L.1
  • 22
    • 34547555144 scopus 로고    scopus 로고
    • Selectivity principle of the ligand escape process from a two-gate tunnel in myoglobin: Molecular dynamics simulation
    • Sheu SY (2006) Selectivity principle of the ligand escape process from a two-gate tunnel in myoglobin: Molecular dynamics simulation. J Chem Phys 124:154711.
    • (2006) J Chem Phys , vol.124 , pp. 154711
    • Sheu, S.Y.1
  • 23
    • 33646177412 scopus 로고    scopus 로고
    • Role of protein flexibility in ion permeation: A case study in gramicidin
    • Bastug T, Gray-Weale A, Patra SM, Kuyucak S (2006) Role of protein flexibility in ion permeation: A case study in gramicidin. Biophys J 90:2285-2296.
    • (2006) Biophys J , vol.90 , pp. 2285-2296
    • Bastug, T.1    Gray-Weale, A.2    Patra, S.M.3    Kuyucak, S.4
  • 24
    • 33747452055 scopus 로고    scopus 로고
    • Probing a water channel near the A-ring of receptor-bound 1α,25-dihydroxyvitamin D3 with selected 2α-substituted analogues
    • Hourai S, et al. (2006) Probing a water channel near the A-ring of receptor-bound 1α,25-dihydroxyvitamin D3 with selected 2α-substituted analogues. J Med Chem 49:5199-5205.
    • (2006) J Med Chem , vol.49 , pp. 5199-5205
    • Hourai, S.1
  • 25
    • 0038779277 scopus 로고    scopus 로고
    • Structural evaluation of the agonistic action of a vitamin D analog with two side chains binding to the nuclear vitamin D receptor
    • Vaisanen S, Perakyla M, Karkkainen JI, Uskokovic MR, Carlberg C (2003) Structural evaluation of the agonistic action of a vitamin D analog with two side chains binding to the nuclear vitamin D receptor. Mol Pharmacol 63:1230-1237.
    • (2003) Mol Pharmacol , vol.63 , pp. 1230-1237
    • Vaisanen, S.1    Perakyla, M.2    Karkkainen, J.I.3    Uskokovic, M.R.4    Carlberg, C.5
  • 26
    • 33744513944 scopus 로고    scopus 로고
    • Vitamin D receptor agonists specifically modulate the volume of the ligand-binding pocket
    • Molnar F, Perakyla M, Carlberg C (2006) Vitamin D receptor agonists specifically modulate the volume of the ligand-binding pocket. J Biol Chem 281:10516-10526.
    • (2006) J Biol Chem , vol.281 , pp. 10516-10526
    • Molnar, F.1    Perakyla, M.2    Carlberg, C.3
  • 27
    • 33746331105 scopus 로고    scopus 로고
    • Detailed molecular understanding of agonistic and antagonistic vitamin D receptor ligands
    • Carlberg C, Molnar F (2006) Detailed molecular understanding of agonistic and antagonistic vitamin D receptor ligands. Curr Top Med Chem 6:1243-1253.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1243-1253
    • Carlberg, C.1    Molnar, F.2
  • 28
    • 0032906662 scopus 로고    scopus 로고
    • Unbinding of retinoic acid from its receptor studied by steered molecular dynamics
    • Kosztin D, Izrailev S, Schulten K (1999) Unbinding of retinoic acid from its receptor studied by steered molecular dynamics. Biophys J 76:188-197.
    • (1999) Biophys J , vol.76 , pp. 188-197
    • Kosztin, D.1    Izrailev, S.2    Schulten, K.3
  • 29
    • 0004752110 scopus 로고    scopus 로고
    • Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α or estrogen receptor-β
    • Sun J, et al. (1999) Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α or estrogen receptor-β. Endocrinology 140:800-804.
    • (1999) Endocrinology , vol.140 , pp. 800-804
    • Sun, J.1
  • 30
    • 0036234964 scopus 로고    scopus 로고
    • Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism
    • Shiau AK, et al. (2002) Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism. Nat Struct Biol 9:359-364.
    • (2002) Nat Struct Biol , vol.9 , pp. 359-364
    • Shiau, A.K.1
  • 31
    • 19944426059 scopus 로고    scopus 로고
    • Thyroxine-thyroid hormone receptor interactions
    • Sandler B, et al. (2004) Thyroxine-thyroid hormone receptor interactions. J Biol Chem 279:55801-55808.
    • (2004) J Biol Chem , vol.279 , pp. 55801-55808
    • Sandler, B.1
  • 32
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics
    • Waldron TT, Murphy KP (2003) Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics. Biochemistry 42:5058-5064.
    • (2003) Biochemistry , vol.42 , pp. 5058-5064
    • Waldron, T.T.1    Murphy, K.P.2
  • 33
    • 52049123291 scopus 로고    scopus 로고
    • Doenthalpy and entropy distinguish first in class from best in class?
    • Freire E (2008)Doenthalpy and entropy distinguish first in class from best in class? Drug Disc Today 13:869-874.
    • (2008) Drug Disc Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 34
    • 33745670369 scopus 로고    scopus 로고
    • Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function
    • Nascimento AS, et al. (2006) Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J Mol Biol 360:586-598.
    • (2006) J Mol Biol , vol.360 , pp. 586-598
    • Nascimento, A.S.1
  • 35
    • 21844450222 scopus 로고    scopus 로고
    • Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5′,5-triiodo-L-thyronine and inhibit homodimer formation
    • Togashi M, Nguyen P, Fletterick R, Baxter JD, Webb P (2005) Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5′,5-triiodo-L-thyronine and inhibit homodimer formation. J Biol Chem 280:25665-25673.
    • (2005) J Biol Chem , vol.280 , pp. 25665-25673
    • Togashi, M.1    Nguyen, P.2    Fletterick, R.3    Baxter, J.D.4    Webb, P.5
  • 36
    • 69949118458 scopus 로고    scopus 로고
    • PACKMOL: A package for building initial configurations for molecular dynamics simulations
    • Martinez L, Andrade R, Birgin EG, Martinez JM (2009) PACKMOL: A package for building initial configurations for molecular dynamics simulations. J Comput Chem 30:2157-2164.
    • (2009) J Comput Chem , vol.30 , pp. 2157-2164
    • Martinez, L.1    Andrade, R.2    Birgin, E.G.3    Martinez, J.M.4
  • 37
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips JC, et al. (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26:1781-1802.
    • (2005) J Comput Chem , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 38
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102:3586-3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 39
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr D 50:178-185.
    • (1994) Acta Crystallogr D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.