메뉴 건너뛰기




Volumn 77, Issue 3, 2019, Pages 227-243

Introducing a New Model of Sweet Taste Receptor, a Class C G-protein Coupled Receptor (C GPCR)

Author keywords

C GPCR; Homology modeling; Sweet taste receptor; T1R2; T1R3

Indexed keywords

ASPARTAME; G PROTEIN COUPLED RECEPTOR; TASTE RECEPTORS, TYPE 1;

EID: 85065643703     PISSN: 10859195     EISSN: 15590283     Source Type: Journal    
DOI: 10.1007/s12013-019-00872-7     Document Type: Article
Times cited : (15)

References (57)
  • 3
    • 80053459477 scopus 로고    scopus 로고
    • Gustatory and extragustatory functions of mammalian taste receptors
    • Behrens, M., & Meyerhof, W. (2011). Gustatory and extragustatory functions of mammalian taste receptors. Physiology and Behavior, 105(1), 4–13. 10.1016/j.physbeh.2011.02.010.
    • (2011) Physiology and Behavior , vol.105 , Issue.1 , pp. 4-13
    • Behrens, M.1    Meyerhof, W.2
  • 4
    • 84902271945 scopus 로고    scopus 로고
    • Functional roles of the sweet taste receptor in oral and extraoral tissues
    • Laffitte, A., Neiers, F., & Briand, L. (2014). Functional roles of the sweet taste receptor in oral and extraoral tissues. Current Opinion in Clinical Nutrition and Metabolic Care, 17(4), 379–385. 10.1097/mco.0000000000000058.
    • (2014) Current Opinion in Clinical Nutrition and Metabolic Care , vol.17 , Issue.4 , pp. 379-385
    • Laffitte, A.1    Neiers, F.2    Briand, L.3
  • 7
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • Muto, T., Tsuchiya, D., Morikawa, K., & Jingami, H. (2007). Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proceedings of the National Academy of Sciences, 104(10), 3759–3764.
    • (2007) Proceedings of the National Academy of Sciences , vol.104 , Issue.10 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 9
    • 84930646504 scopus 로고    scopus 로고
    • Engineering G protein-coupled receptors for drug design
    • (,).,., G., Scapin, D., Patel, E., Arnold, (Eds),. (pp)., Netherlands,:, Springer,., https://doi.org/10.1007/978-94-017-9719-1
    • Congreve, M., Doré, A.S., Jazayeri, A., Nonoo, R. (2015). Engineering G protein-coupled receptors for drug design. In G. Scapin, D. Patel, E. Arnold (Eds), Multifaceted roles of crystallography in modern drug discovery. (pp 1–18). Netherlands: Springer. 10.1007/978-94-017-9719-1.
    • (2015) Multifaceted roles of crystallography in modern drug discovery , pp. 1-18
    • Congreve, M.1    Doré, A.S.2    Jazayeri, A.3    Nonoo, R.4
  • 10
    • 3242813635 scopus 로고    scopus 로고
    • Utility of homology models in the drug discovery process
    • Hillisch, A. (2004). Utility of homology models in the drug discovery process. Drug Discovery Today., 9, 659–69.
    • (2004) Drug Discovery Today. , vol.9 , pp. 659-669
    • Hillisch, A.1
  • 11
    • 33751505567 scopus 로고    scopus 로고
    • The heterodimeric sweet taste receptor has multiple potential ligand binding sites
    • Cui, M., Jiang, P., Maillet, E., Max, M., Margolskee, R. F., & Osman, R. (2006). The heterodimeric sweet taste receptor has multiple potential ligand binding sites. Current Pharmaceutical Design, 12(35), 4591–4600. 10.2174/138161206779010350.
    • (2006) Current Pharmaceutical Design , vol.12 , Issue.35 , pp. 4591-4600
    • Cui, M.1    Jiang, P.2    Maillet, E.3    Max, M.4    Margolskee, R.F.5    Osman, R.6
  • 14
    • 85014624308 scopus 로고    scopus 로고
    • Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists
    • Kim, S.-K., Chen, Y., Abrol, R., Goddard, W. A., & Guthrie, B. (2017). Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists. Proceedings of the National Academy of Sciences, 114(10), 2568–2573. 10.1073/pnas.1700001114.
    • (2017) Proceedings of the National Academy of Sciences , vol.114 , Issue.10 , pp. 2568-2573
    • Kim, S.K.1    Chen, Y.2    Abrol, R.3    Goddard, W.A.4    Guthrie, B.5
  • 15
    • 26644458124 scopus 로고    scopus 로고
    • Identification of the cyclamate interaction site within the transmembrane domain of the human sweet taste receptor subunit T1R3
    • Jiang, P. H., Cui, M., Zhao, B. H., Snyder, L. A., Benard, L. M. J., Osman, R., Max, M., & Margolskee, R. F. (2005). Identification of the cyclamate interaction site within the transmembrane domain of the human sweet taste receptor subunit T1R3. Journal of Biological Chemistry, 280(40), 34296–34305. 10.1074/jbc.M505255200.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 34296-34305
    • Jiang, P.H.1    Cui, M.2    Zhao, B.H.3    Snyder, L.A.4    Benard, L.M.J.5    Osman, R.6    Max, M.7    Margolskee, R.F.8
  • 17
    • 36749099088 scopus 로고    scopus 로고
    • The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor
    • Winnig, M., Bufe, B., Kratochwil, N. A., Slack, J. P., & Meyerhof, W. (2007). The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor. BMC Structural Biology, 7, 66 10.1186/1472-6807-7-66.
    • (2007) BMC Structural Biology , vol.7
    • Winnig, M.1    Bufe, B.2    Kratochwil, N.A.3    Slack, J.P.4    Meyerhof, W.5
  • 19
    • 77951901176 scopus 로고    scopus 로고
    • Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor
    • Assadi-Porter, F. M., Maillet, E. L., Radek, J. T., Quijada, J., Markley, J. L., & Max, M. (2010). Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor. Journal of Molecular Biology, 398(4), 584–599. 10.1016/j.jmb.2010.03.017.
    • (2010) Journal of Molecular Biology , vol.398 , Issue.4 , pp. 584-599
    • Assadi-Porter, F.M.1    Maillet, E.L.2    Radek, J.T.3    Quijada, J.4    Markley, J.L.5    Max, M.6
  • 20
    • 84859986450 scopus 로고    scopus 로고
    • Characterization of the modes of binding between human sweet taste receptor and low-molecular-weight sweet compounds
    • Masuda, K., Koizumi, A., Nakajima K-i, Tanaka, T., Abe, K., Misaka, T., & Ishiguro, M. (2012). Characterization of the modes of binding between human sweet taste receptor and low-molecular-weight sweet compounds. PLoS ONE, 7(4), e35380 10.1371/journal.pone.0035380.
    • (2012) PLoS ONE , vol.7 , Issue.4
    • Masuda, K.1    Koizumi, A.2    Nakajima K-i3    Tanaka, T.4    Abe, K.5    Misaka, T.6    Ishiguro, M.7
  • 22
    • 84935005759 scopus 로고    scopus 로고
    • Interaction model of steviol glycosides from Stevia rebaudiana (Bertoni) with sweet taste receptors: a computational approach
    • Mayank, JaitakV. (2015). Interaction model of steviol glycosides from Stevia rebaudiana (Bertoni) with sweet taste receptors: a computational approach. Phytochemistry, 116(1), 12–20. 10.1016/j.phytochem.2015.05.006.
    • (2015) Phytochemistry , vol.116 , Issue.1 , pp. 12-20
    • Mayank, J.V.1
  • 24
  • 28
    • 85016153986 scopus 로고    scopus 로고
    • UniProt: the universal protein knowledgebase
    • Consortium, T. U. (2017). UniProt: the universal protein knowledgebase. Nucleic Acids Research, 45(D1), D158–D169. 10.1093/nar/gkw1099.
    • (2017) Nucleic Acids Research , vol.45 , Issue.D1 , pp. D158-D169
    • Consortium, T.U.1
  • 30
    • 84908088475 scopus 로고    scopus 로고
    • YASARA View—molecular graphics for all devices—from smartphones to workstations
    • Krieger, E., & Vriend, G. (2014). YASARA View—molecular graphics for all devices—from smartphones to workstations. Bioinformatics, 30(20), 2981–2982.
    • (2014) Bioinformatics , vol.30 , Issue.20 , pp. 2981-2982
    • Krieger, E.1    Vriend, G.2
  • 32
    • 0030047142 scopus 로고    scopus 로고
    • Errors in protein structures
    • Hooft, R. W., Vriend, G., Sander, C., & Abola, E. E. (1996). Errors in protein structures. Nature, 381(6580), 272.
    • (1996) Nature , vol.381 , Issue.6580 , pp. 272
    • Hooft, R.W.1    Vriend, G.2    Sander, C.3    Abola, E.E.4
  • 33
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinformatics, 9(1), 1–8. 10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , Issue.1 , pp. 1-8
    • Zhang, Y.1
  • 34
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., & Zhang, Y. (2010). I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols, 5(4), 725–738.
    • (2010) Nature Protocols , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 35
    • 84938745406 scopus 로고    scopus 로고
    • GPCR-I-TASSER: a hybrid approach to G protein-coupled receptor structure modeling and the application to the human genome
    • Zhang, J., Yang, J., Jang, R., & Zhang, Y. (2015). GPCR-I-TASSER: a hybrid approach to G protein-coupled receptor structure modeling and the application to the human genome. Structure, 23(8), 1538–1549. 10.1016/j.str.2015.06.007.
    • (2015) Structure , vol.23 , Issue.8 , pp. 1538-1549
    • Zhang, J.1    Yang, J.2    Jang, R.3    Zhang, Y.4
  • 36
    • 84907676331 scopus 로고    scopus 로고
    • A 3D model for human melanocortin 4 receptor refined with molecular dynamics simulation
    • Shahlaei, M., & Mousavi, A. (2014). A 3D model for human melanocortin 4 receptor refined with molecular dynamics simulation. Journal of Reports in Pharmaceutical Sciences, 3(1), 42–53.
    • (2014) Journal of Reports in Pharmaceutical Sciences , vol.3 , Issue.1 , pp. 42-53
    • Shahlaei, M.1    Mousavi, A.2
  • 37
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. (1999). Protein secondary structure prediction based on position-specific scoring matrices. Journal of Molecular Biology, 292(2), 195–202.
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 38
    • 84979854249 scopus 로고    scopus 로고
    • JPred4: a protein secondary structure prediction server
    • Drozdetskiy, A., Cole, C., Procter, J., & Barton, G. J. (2015). JPred4: a protein secondary structure prediction server. Nucleic Acids Research, 43(W1), W389–W394. 10.1093/nar/gkv332.
    • (2015) Nucleic Acids Research , vol.43 , Issue.W1 , pp. W389-W394
    • Drozdetskiy, A.1    Cole, C.2    Procter, J.3    Barton, G.J.4
  • 39
    • 0029595442 scopus 로고
    • SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon, C., & Deléage, G. (1995). SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Computer Applications in the Biosciences, 11(6), 681–684. 10.1093/bioinformatics/11.6.681.
    • (1995) Computer Applications in the Biosciences , vol.11 , Issue.6 , pp. 681-684
    • Geourjon, C.1    Deléage, G.2
  • 40
    • 84880998440 scopus 로고    scopus 로고
    • Porter, PaleAle 4.0: high-accuracy prediction of protein secondary structure and relative solvent accessibility
    • Mirabello, C., & Pollastri, G. (2013). Porter, PaleAle 4.0: high-accuracy prediction of protein secondary structure and relative solvent accessibility. Bioinformatics, 29(16), 2056–2058.
    • (2013) Bioinformatics , vol.29 , Issue.16 , pp. 2056-2058
    • Mirabello, C.1    Pollastri, G.2
  • 41
    • 85061313845 scopus 로고    scopus 로고
    • A systematic review on popularity, application and characteristics of protein secondary structure prediction tools
    • (,),.,., https://doi.org/10.2174/1570163815666180227162157
    • Kashani-Amin, E., Tabatabaei-Malazy, O., Sakhteman, A., Larijani, B., Ebrahim-Habibi, A. (2018) A systematic review on popularity, application and characteristics of protein secondary structure prediction tools. Current Drug Discovery Technologies, 15. 10.2174/1570163815666180227162157
    • (2018) Current Drug Discovery Technologies , vol.15
    • Kashani-Amin, E.1    Tabatabaei-Malazy, O.2    Sakhteman, A.3    Larijani, B.4    Ebrahim-Habibi, A.5
  • 43
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund, H., & Elofsson, A. (2008). OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics, 24(15), 1662–1668.
    • (2008) Bioinformatics , vol.24 , Issue.15 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 44
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • In
    • Sonnhammer E.L., Von Heijne G., Krogh A. A hidden Markov model for predicting transmembrane helices in protein sequences. In: Ismb, 1998. pp 175-182
    • (1998) Ismb , pp. 175-182
    • Sonnhammer, E.L.1    Von Heijne, G.2    Krogh, A.3
  • 45
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8
    • Krieger, E., Joo, K., Lee, J., Lee, J., Raman, S., Thompson, J., Tyka, M., Baker, D., & Karplus, K. (2009). Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8. Proteins, 77(Suppl 9), 114–122. 10.1002/prot.22570.
    • (2009) Proteins , vol.77 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6    Tyka, M.7    Baker, D.8    Karplus, K.9
  • 47
    • 84928476077 scopus 로고    scopus 로고
    • New ways to boost molecular dynamics simulations
    • Krieger, E., & Vriend, G. (2015). New ways to boost molecular dynamics simulations. Journal of Computational Chemistry, 36(13), 996–1007.
    • (2015) Journal of Computational Chemistry , vol.36 , Issue.13 , pp. 996-1007
    • Krieger, E.1    Vriend, G.2
  • 51
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O., & Olson, A. J. (2010). AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461.
    • (2010) Journal of Computational Chemistry , vol.31 , Issue.2 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 52
    • 0242663237 scopus 로고    scopus 로고
    • A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculations
    • Duan, Y., Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang, W., Yang, R., Cieplak, P., Luo, R., & Lee, T. (2003). A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculations. Journal of Computational Chemistry, 24(16), 1999–2012.
    • (2003) Journal of Computational Chemistry , vol.24 , Issue.16 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10
  • 53
    • 61449104961 scopus 로고    scopus 로고
    • Fragment-based identification of druggable ‘hot spots’ of proteins using Fourier domain correlation techniques
    • Brenke, R., Kozakov, D., Chuang, G.-Y., Beglov, D., Hall, D., Landon, M. R., Mattos, C., & Vajda, S. (2009). Fragment-based identification of druggable ‘hot spots’ of proteins using Fourier domain correlation techniques. Bioinformatics, 25(5), 621–627.
    • (2009) Bioinformatics , vol.25 , Issue.5 , pp. 621-627
    • Brenke, R.1    Kozakov, D.2    Chuang, G.Y.3    Beglov, D.4    Hall, D.5    Landon, M.R.6    Mattos, C.7    Vajda, S.8
  • 55


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.