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Volumn 49, Issue 11, 2006, Pages 3077-3085

Construction of human ghrelin receptor (hGHS-R1a) model using a fragmental prediction approach and validation through docking analysis

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GHRELIN; GHRELIN RECEPTOR; GROWTH HORMONE; HORMONE RECEPTOR; INDAN DERIVATIVE; INDOLE DERIVATIVE; RHODOPSIN; SPIRO COMPOUND; TETRAPEPTIDE; UNCLASSIFIED DRUG;

EID: 33744814084     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm058053k     Document Type: Article
Times cited : (28)

References (54)
  • 3
    • 0018899801 scopus 로고
    • Structure-activity relationships of a synthetic pentapeptide that specifically releases growth hormone in vitro
    • Bowers, C. Y.; Momany, F.; Reynolds, G. A.; Chang, D.; Hong, A.; Chang, K. Structure-activity relationships of a synthetic pentapeptide that specifically releases growth hormone in vitro. Endocrinology 1980, 106, 663-667.
    • (1980) Endocrinology , vol.106 , pp. 663-667
    • Bowers, C.Y.1    Momany, F.2    Reynolds, G.A.3    Chang, D.4    Hong, A.5    Chang, K.6
  • 5
    • 33744830519 scopus 로고    scopus 로고
    • note
    • The complete amino acidic sequence of ghrelin is GSS(octanoil)- FLSPEHQRVQQRKESKKPPAKLQPR.
  • 6
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • Kojima, M.; Hosoda, H.; Date, Y.; Nakazato, M.; Matsuo, H.; Kangawa, K. Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 1999, 402, 656-660.
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 7
    • 0035860282 scopus 로고    scopus 로고
    • Structure-activity relationship of ghrelin: Pharmacological study of ghrelin peptides
    • Matsumoto, M.; Hosoda, H.; Morizumi, N.; Hayashi, Y. Structure-activity relationship of ghrelin: pharmacological study of ghrelin peptides. Biochem. Biophys. Res. Commun. 2001, 287, 142-146.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 142-146
    • Matsumoto, M.1    Hosoda, H.2    Morizumi, N.3    Hayashi, Y.4
  • 8
    • 15544385058 scopus 로고    scopus 로고
    • Ghrelin: Structure and function
    • Kojima, M.; Kangawa, K. Ghrelin: structure and function. Physiol. Reu. 2005, 85, 495-522.
    • (2005) Physiol. Reu. , vol.85 , pp. 495-522
    • Kojima, M.1    Kangawa, K.2
  • 9
    • 24044505417 scopus 로고    scopus 로고
    • The many faces of ghrelin: New perspectives for nutrition research?
    • Otto, B.; Spranger, J.; Benoit, S. C.; Clegg, D. J.; Tschop, M. H. The many faces of ghrelin: new perspectives for nutrition research? Br. J. Nutr. 2005, 93, 765-771.
    • (2005) Br. J. Nutr. , vol.93 , pp. 765-771
    • Otto, B.1    Spranger, J.2    Benoit, S.C.3    Clegg, D.J.4    Tschop, M.H.5
  • 10
    • 11144262776 scopus 로고    scopus 로고
    • Ghrelin: A gastric peptide that regulates food intake and energy homeostasis
    • Ueno, H.; Yamaguchi, H.; Kangawa, K.; Nakazato, M., Ghrelin: a gastric peptide that regulates food intake and energy homeostasis. Regul. Pept. 2005, 126, 11-19.
    • (2005) Regul. Pept. , vol.126 , pp. 11-19
    • Ueno, H.1    Yamaguchi, H.2    Kangawa, K.3    Nakazato, M.4
  • 11
    • 2942528459 scopus 로고    scopus 로고
    • Biological, physiological, pathophysiological, and pharmacological aspects of ghrelin
    • van der Lely, A. J.; Tschop, M.; Heiman, M. L.; Ghigo, E. Biological, physiological, pathophysiological, and pharmacological aspects of ghrelin. Endocr. Rev. 2004, 25, 426-457.
    • (2004) Endocr. Rev. , vol.25 , pp. 426-457
    • Van Der Lely, A.J.1    Tschop, M.2    Heiman, M.L.3    Ghigo, E.4
  • 12
    • 18844404431 scopus 로고    scopus 로고
    • Development of growth hormone secretagogues
    • Smith, R. G. Development of growth hormone secretagogues. Endocr. Rev. 2005, 26, 346-360.
    • (2005) Endocr. Rev. , vol.26 , pp. 346-360
    • Smith, R.G.1
  • 13
    • 15444371950 scopus 로고    scopus 로고
    • Overduin, Ghrelin and energy balance: Focus on current controversies
    • Cummings, D. E.; Foster-Schubert, K. E.; Overduin, Ghrelin and energy balance: focus on current controversies. J. Curr. Drug. Targets 2005, 6, 153-169.
    • (2005) J. Curr. Drug. Targets , vol.6 , pp. 153-169
    • Cummings, D.E.1    Foster-Schubert, K.E.2
  • 17
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • Holst, B.; Holliday, N. D.; Bach, A.; Elling, C. E.; Cox, H. M.; Schwartz, T. W. Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 2004, 279, 53806-53817.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53806-53817
    • Holst, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 18
    • 0034998144 scopus 로고    scopus 로고
    • Genomic structure and transcriptional regulation of the human growth hormone secretagogue receptor
    • Petersenn, S.; Rasch, A. C.; Penshorn, M.; Beil, F. U.; Schulte, H. M. Genomic structure and transcriptional regulation of the human growth hormone secretagogue receptor. Endocrinology 2001, 142, 2649-2659.
    • (2001) Endocrinology , vol.142 , pp. 2649-2659
    • Petersenn, S.1    Rasch, A.C.2    Penshorn, M.3    Beil, F.U.4    Schulte, H.M.5
  • 19
    • 33744805298 scopus 로고    scopus 로고
    • note
    • In this article, the residues are progressively numbered from 1 to 366, irrespective of the corresponding segment.
  • 21
    • 0242330291 scopus 로고    scopus 로고
    • High constitutive signaling of the ghrelin receptor-identification of a potent inverse agonist
    • Holst, B.; Cygankiewicz, A.; Jensen, T. H.; Ankersen, M.; Schwartz, T. W. High constitutive signaling of the ghrelin receptor-identification of a potent inverse agonist. Mol. Endocrinol. 2003, 17, 2201-2210.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2201-2210
    • Holst, B.1    Cygankiewicz, A.2    Jensen, T.H.3    Ankersen, M.4    Schwartz, T.W.5
  • 22
    • 0033607270 scopus 로고    scopus 로고
    • Conversion of agonist site to metal-ion chelator site in the beta(2)-adrenergic receptor
    • Elling, C. E.; Thirstrup, K.; Holst, B.; Schwartz, T. W. Conversion of agonist site to metal-ion chelator site in the beta(2)-adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 12322-12327.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12322-12327
    • Elling, C.E.1    Thirstrup, K.2    Holst, B.3    Schwartz, T.W.4
  • 23
    • 0037494099 scopus 로고    scopus 로고
    • The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors
    • Filipek, S.; Teller, D. C.; Palczewski, K.; Stenkamp, R. The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors. Annu. Rev. Biophys. Biomol. Struct. 2003, 32, 375-397
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 375-397
    • Filipek, S.1    Teller, D.C.2    Palczewski, K.3    Stenkamp, R.4
  • 24
    • 25444444202 scopus 로고    scopus 로고
    • Computational modeling approaches to structure-function analysis of G protein-coupled receptors
    • Fanelli, F.; De Benedetti, P. G. Computational modeling approaches to structure-function analysis of G protein-coupled receptors. Chem. Rev. 2005, 105, 3297-3351.
    • (2005) Chem. Rev. , vol.105 , pp. 3297-3351
    • Fanelli, F.1    De Benedetti, P.G.2
  • 25
    • 23944454816 scopus 로고    scopus 로고
    • Virtual screening of biogenic amine-binding G-protein coupled receptors: Comparative evaluation of protein- and ligand-based virtual screening protocols
    • and references cited herein
    • Evers, A.; Hessler, G.; Matter, H.; Klabunde, T. Virtual screening of biogenic amine-binding G-protein coupled receptors: Comparative evaluation of protein- and ligand-based virtual screening protocols, J. Med. Chem., 2005, 48, 5448-5465 and references cited herein.
    • (2005) J. Med. Chem. , vol.48 , pp. 5448-5465
    • Evers, A.1    Hessler, G.2    Matter, H.3    Klabunde, T.4
  • 28
    • 0037624841 scopus 로고    scopus 로고
    • 3D-Shotgun: A novel cooperative fold-recognition metapredictor
    • Fischer, D. 3D-Shotgun: a novel cooperative fold-recognition metapredictor, Proteins, 2003, 51, 434-441.
    • (2003) Proteins , vol.51 , pp. 434-441
    • Fischer, D.1
  • 29
    • 0034676324 scopus 로고    scopus 로고
    • Structure-function studies on the new growth hormone-releasing peptide, ghrelin: Minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a
    • Bednarek, M. A.; Feighner, S. D.; Pong, S. S.; McKee, K. K.; Hreniuk, D. L.; Silva, M. V.; Warren, V. A.; Howard, A. D.; van Der Ploeg, L. H.; Heck, J. V. Structure-function studies on the new growth hormone-releasing peptide, ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a. J. Med. Chem. 2000, 43, 4370-4376.
    • (2000) J. Med. Chem. , vol.43 , pp. 4370-4376
    • Bednarek, M.A.1    Feighner, S.D.2    Pong, S.S.3    McKee, K.K.4    Hreniuk, D.L.5    Silva, M.V.6    Warren, V.A.7    Howard, A.D.8    Van Der Ploeg, L.H.9    Heck, J.V.10
  • 30
    • 0035895421 scopus 로고    scopus 로고
    • Nonalphahelical elements modulate polytopic membrane protein architecture
    • Riek, R. P.; Rigoutsos, I.; Novotny, J.; Graham, R. M. Nonalphahelical elements modulate polytopic membrane protein architecture. J. Mol. Biol. 2001, 306, 349-362.
    • (2001) J. Mol. Biol. , vol.306 , pp. 349-362
    • Riek, R.P.1    Rigoutsos, I.2    Novotny, J.3    Graham, R.M.4
  • 31
    • 33744806581 scopus 로고    scopus 로고
    • note
    • The average distance between a pair of helices was calculated by averaging the lowest distances obtained considering all possible residues of the second helix for each residue of the first helix. The position of each residue is defined only by the Cα atom.
  • 34
    • 2642548891 scopus 로고    scopus 로고
    • Binding site analysis of full-length alpha(1a) adrenergic receptor using homology modeling and molecular docking
    • Pedretti, A.; Silva, M. E.; Villa, L.; Vistoli, G. Binding site analysis of full-length alpha(1a) adrenergic receptor using homology modeling and molecular docking. Biochem. Biophys. Res. Commun. 2004, 310, 1083-1088.
    • (2004) Biochem. Biophys. Res. Commun. , vol.310 , pp. 1083-1088
    • Pedretti, A.1    Silva, M.E.2    Villa, L.3    Vistoli, G.4
  • 35
    • 0037155845 scopus 로고    scopus 로고
    • Differential determinants for peptide and nonpeptidyl ligand binding to the Motilin receptor
    • Matsuura, B.; Dong, M.; Miller, L. J. Differential determinants for peptide and nonpeptidyl ligand binding to the Motilin receptor. J. Biol. Chem. 2002, 277, 9834-9839.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9834-9839
    • Matsuura, B.1    Dong, M.2    Miller, L.J.3
  • 36
    • 33744831101 scopus 로고    scopus 로고
    • note
    • ftp://dasher.wustl.edu/pub/qsar.
  • 37
    • 24344479915 scopus 로고    scopus 로고
    • Nonpeptide and peptide growth hormone secretagogues act both as ghrelin receptor agonist and as positive or negative allosteric modulators of ghrelin signaling
    • Holst, B.; Brandt, E.; Bach, A.; Heding, A.; Schwartz, T. W. Nonpeptide and peptide growth hormone secretagogues act both as ghrelin receptor agonist and as positive or negative allosteric modulators of ghrelin signaling. Mol. Endocrinol. 2005, 19, 2400-2411.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2400-2411
    • Holst, B.1    Brandt, E.2    Bach, A.3    Heding, A.4    Schwartz, T.W.5
  • 38
    • 33744829979 scopus 로고    scopus 로고
    • http://www.expasy.org/uniprot/GHSR_HUMAN.
  • 39
    • 33744829441 scopus 로고    scopus 로고
    • http://www.ch.embnet.org/software/TMPRED_form.html.
  • 40
    • 33744812661 scopus 로고    scopus 로고
    • note
    • The sequence fragmentation was also performed using other approaches (DAS, KKD, SOSU1, TMHMM, HMMTOP) obtaining results that were quite identical.
  • 41
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi, J.; Blundell, T. L.; Mizuguchi, K., FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 2001, 310, 243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 43
    • 0036284090 scopus 로고    scopus 로고
    • VEGA: A versatile program to convert, handle and visualize molecular structure on windows-based PCs
    • Pedretti, A.; Villa, L.; Vistoli, G. VEGA: a versatile program to convert, handle and visualize molecular structure on windows-based PCs. J. Mol. Graphics Modell. 2002, 21, 47-49.
    • (2002) J. Mol. Graphics Modell. , vol.21 , pp. 47-49
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 44
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 45
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U.; Luthy, R.; Eisenberg, D. A method to identify protein sequences that fold into a known three-dimensional structure. Science. 1991, 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 47
    • 0021997308 scopus 로고
    • An extremely sensitive in vitro model for elucidating structure-activity relationships of growth hormone-releasing factor analogues
    • Heiman, M. L.; Nekola, M. V.; Murphy, W. A.; Lance, V. A.; Coy, D. H. An extremely sensitive in vitro model for elucidating structure-activity relationships of growth hormone-releasing factor analogues, Endocrinology 1985, 116, 410-415.
    • (1985) Endocrinology , vol.116 , pp. 410-415
    • Heiman, M.L.1    Nekola, M.V.2    Murphy, W.A.3    Lance, V.A.4    Coy, D.H.5
  • 51
    • 7344221463 scopus 로고    scopus 로고
    • 1-[2(R)-(2-amino-2-methylpropionylamino)-3-(1H-indol-3-yl)propionyl]- 3-benzylpiperidine-3(S)-carboxylic acid ethyl ester (L-163, 540): A potent, orally bioavailable, and short-duration growth hormone secretagogue
    • Yang, L.; Morriello, G.; Patchett, A. A.; Leung, K.; Jacks, T.; Cheng, K.; Schleim, K. D.; Feeney, W.; Chan, W. W.; Chiu, S. H.; Smith, R. G., 1-[2(R)-(2-amino-2-methylpropionylamino)-3-(1H-indol-3-yl)propionyl]- 3-benzylpiperidine-3(S)-carboxylic acid ethyl ester (L-163, 540): a potent, orally bioavailable, and short-duration growth hormone secretagogue. J. Med. Chem. 1998, 41, 2439-2441.
    • (1998) J. Med. Chem. , vol.41 , pp. 2439-2441
    • Yang, L.1    Morriello, G.2    Patchett, A.A.3    Leung, K.4    Jacks, T.5    Cheng, K.6    Schleim, K.D.7    Feeney, W.8    Chan, W.W.9    Chiu, S.H.10    Smith, R.G.11
  • 54
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey, M.; Kramer, B.; Lengauer, T.; Klebe, G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 1996, 261, 470-489.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4


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