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Volumn 24, Issue 7, 2017, Pages 570-577

Structural basis for the cooperative allosteric activation of the free fatty acid receptor GPR40

(34)  Lu, Jun a   Byrne, Noel a   Wang, John a   Bricogne, Gerard b   Brown, Frank K a   Chobanian, Harry R a   Colletti, Steven L a   Di Salvo, Jerry a   Thomas Fowlkes, Brande a   Guo, Yan a   Hall, Dawn L a   Hadix, Jennifer a   Hastings, Nicholas B a   Hermes, Jeffrey D a   Ho, Thu a   Howard, Andrew D a   Josien, Hubert a   Kornienko, Maria a   Lumb, Kevin J a   Miller, Michael W a   more..


Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC AGONIST; ANTIDIABETIC AGENT; G PROTEIN COUPLED RECEPTOR 40; LIPID; MK 8666; PARTIAL AGONIST; UNCLASSIFIED DRUG; FFAR1 PROTEIN, HUMAN; G PROTEIN COUPLED RECEPTOR; PROTEIN BINDING;

EID: 85022332317     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3417     Document Type: Article
Times cited : (153)

References (31)
  • 1
    • 84897554321 scopus 로고    scopus 로고
    • G-protein coupled receptor 40 agonists as novel therapeutics for type 2 diabetes
    • Choi, Y.J., Shin, D. & Lee, J.Y. G-protein coupled receptor 40 agonists as novel therapeutics for type 2 diabetes. Arch. Pharm. Res. 37, 435-439 (2014).
    • (2014) Arch. Pharm. Res , vol.37 , pp. 435-439
    • Choi, Y.J.1    Shin, D.2    Lee, J.Y.3
  • 2
    • 0037423719 scopus 로고    scopus 로고
    • A human cell surface receptor activated by free fatty acids and thiazolidinedione drugs
    • Kotarsky, K., Nilsson, N.E., Flodgren, E., Owman, C. & Olde, B. A human cell surface receptor activated by free fatty acids and thiazolidinedione drugs. Biochem. Biophys. Res. Commun. 301, 406-410 (2003).
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 406-410
    • Kotarsky, K.1    Nilsson, N.E.2    Flodgren, E.3    Owman, C.4    Olde, B.5
  • 3
    • 33846327180 scopus 로고    scopus 로고
    • GPR40 is expressed in glucagon producing cells and affects glucagon secretion
    • Flodgren, E. et al. GPR40 is expressed in glucagon producing cells and affects glucagon secretion. Biochem. Biophys. Res. Commun. 354, 240-245 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.354 , pp. 240-245
    • Flodgren, E.1
  • 5
    • 84867306794 scopus 로고    scopus 로고
    • Identification and pharmacological characterization of multiple allosteric binding sites on the free fatty acid 1 receptor
    • Lin, D.C. et al. Identification and pharmacological characterization of multiple allosteric binding sites on the free fatty acid 1 receptor. Mol. Pharmacol. 82, 843-859 (2012).
    • (2012) Mol. Pharmacol , vol.82 , pp. 843-859
    • Lin, D.C.1
  • 6
    • 84907221192 scopus 로고    scopus 로고
    • High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875
    • Srivastava, A. et al. High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875. Nature 513, 124-127 (2014).
    • (2014) Nature , vol.513 , pp. 124-127
    • Srivastava, A.1
  • 7
    • 84905041106 scopus 로고    scopus 로고
    • Generating thermostabilized agonist-bound GPR40/FFAR1 using virus-like particles and a label-free binding assay
    • Hirozane, Y., Motoyaji, T., Maru, T., Okada, K. & Tarui, N. Generating thermostabilized agonist-bound GPR40/FFAR1 using virus-like particles and a label-free binding assay. Mol. Membr. Biol. 31, 168-175 (2014).
    • (2014) Mol. Membr. Biol , vol.31 , pp. 168-175
    • Hirozane, Y.1    Motoyaji, T.2    Maru, T.3    Okada, K.4    Tarui, N.5
  • 8
    • 84968796800 scopus 로고    scopus 로고
    • Extra-helical binding site of a glucagon receptor antagonist
    • Jazayeri, A. et al. Extra-helical binding site of a glucagon receptor antagonist. Nature 533, 274-277 (2016).
    • (2016) Nature , vol.533 , pp. 274-277
    • Jazayeri, A.1
  • 9
    • 84928469118 scopus 로고    scopus 로고
    • Two disparate ligand-binding sites in the human P2Y1 receptor
    • Zhang, D. et al. Two disparate ligand-binding sites in the human P2Y1 receptor. Nature 520, 317-321 (2015).
    • (2015) Nature , vol.520 , pp. 317-321
    • Zhang, D.1
  • 10
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse, A.C. et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504, 101-106 (2013).
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1
  • 11
    • 84920736359 scopus 로고    scopus 로고
    • GPR40 (FFAR1)-combined Gs and Gq signaling in vitro is associated with robust incretin secretagogue action ex vivo and in vivo
    • Hauge, M. et al. GPR40 (FFAR1)-combined Gs and Gq signaling in vitro is associated with robust incretin secretagogue action ex vivo and in vivo. Mol. Metab. 4, 3-14 (2014).
    • (2014) Mol. Metab , vol.4 , pp. 3-14
    • Hauge, M.1
  • 12
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612, 1-40 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 13
    • 79952316125 scopus 로고    scopus 로고
    • Structure of rhomboid protease in a lipid environment
    • Vinothkumar, K.R. Structure of rhomboid protease in a lipid environment. J. Mol. Biol. 407, 232-247 (2011).
    • (2011) J. Mol. Biol , vol.407 , pp. 232-247
    • Vinothkumar, K.R.1
  • 14
    • 35748937333 scopus 로고    scopus 로고
    • Identification of residues important for agonist recognition and activation in GPR40
    • Sum, C.S. et al. Identification of residues important for agonist recognition and activation in GPR40. J. Biol. Chem. 282, 29248-29255 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 29248-29255
    • Sum, C.S.1
  • 15
    • 84941000099 scopus 로고    scopus 로고
    • Free fatty acid receptors: Structural models and elucidation of ligand binding interactions
    • Tikhonova, I.G. & Poerio, E. Free fatty acid receptors: structural models and elucidation of ligand binding interactions. BMC Struct. Biol. 15, 16 (2015).
    • (2015) BMC Struct. Biol , vol.15 , pp. 16
    • Tikhonova, I.G.1    Poerio, E.2
  • 16
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the '2 adrenergic receptor-Gs protein complex
    • Rasmussen, S.G. et al. Crystal structure of the '2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 17
    • 84938359988 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
    • Kang, Y. et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561-567 (2015).
    • (2015) Nature , vol.523 , pp. 561-567
    • Kang, Y.1
  • 18
    • 84982803363 scopus 로고    scopus 로고
    • Structure of the adenosine A(2A) receptor bound to an engineered G protein
    • Carpenter, B., Nehmé, R., Warne, T., Leslie, A.G. & Tate, C.G. Structure of the adenosine A(2A) receptor bound to an engineered G protein. Nature 536, 104-107 (2016).
    • (2016) Nature , vol.536 , pp. 104-107
    • Carpenter, B.1    Nehmé, R.2    Warne, T.3    Leslie, A.G.4    Tate, C.G.5
  • 19
    • 84939795137 scopus 로고    scopus 로고
    • Structural insights into '-opioid receptor activation
    • Huang, W. et al. Structural insights into '-opioid receptor activation. Nature 524, 315-321 (2015).
    • (2015) Nature , vol.524 , pp. 315-321
    • Huang, W.1
  • 20
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch, V., Cherezov, V. & Stevens, R.C. Structure-function of the G protein-coupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53, 531-556 (2013).
    • (2013) Annu. Rev. Pharmacol. Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 21
    • 84877631485 scopus 로고    scopus 로고
    • Structural features for functional selectivity at serotonin receptors
    • Wacker, D. et al. Structural features for functional selectivity at serotonin receptors. Science 340, 615-619 (2013).
    • (2013) Science , vol.340 , pp. 615-619
    • Wacker, D.1
  • 22
    • 84877607189 scopus 로고    scopus 로고
    • Structural basis for molecular recognition at serotonin receptors
    • Wang, C. et al. Structural basis for molecular recognition at serotonin receptors. Science 340, 610-614 (2013).
    • (2013) Science , vol.340 , pp. 610-614
    • Wang, C.1
  • 23
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan, A.J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185-194 (2013).
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 24
    • 0027379660 scopus 로고
    • Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
    • Moro, O., Lameh, J., Högger, P. & Sadée, W. Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling. J. Biol. Chem. 268, 22273-22276 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 22273-22276
    • Moro, O.1    Lameh, J.2    Högger, P.3    Sadée, W.4
  • 25
    • 0032544633 scopus 로고    scopus 로고
    • The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling
    • Burstein, E.S., Spalding, T.A. & Brann, M.R. The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling. J. Biol. Chem. 273, 24322-24327 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 24322-24327
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 26
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a beta1-adrenergic G-protein-coupled receptor
    • Warne, T. et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 27
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola, V.P. et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211-1217 (2008).
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1
  • 28
    • 84910633308 scopus 로고    scopus 로고
    • A functional selectivity mechanism at the serotonin-2A GPCR involves ligand-dependent conformations of intracellular loop 2
    • Perez-Aguilar, J.M., Shan, J., LeVine, M.V., Khelashvili, G. & Weinstein, H. A functional selectivity mechanism at the serotonin-2A GPCR involves ligand-dependent conformations of intracellular loop 2. J. Am. Chem. Soc. 136, 16044-16054 (2014).
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 16044-16054
    • Perez-Aguilar, J.M.1    Shan, J.2    LeVine, M.V.3    Khelashvili, G.4    Weinstein, H.5
  • 29
    • 84878896978 scopus 로고    scopus 로고
    • The structural basis of G-protein-coupled receptor signaling (nobel lecture
    • Kobilka, B. The structural basis of G-protein-coupled receptor signaling (Nobel Lecture). Angew. Chem. Int. Edn Engl 52 6380-6388 (2013).
    • (2013) Angew. Chem. Int. Edn Engl , vol.52 , pp. 6380-6388
    • Kobilka, B.1
  • 30
    • 84994035484 scopus 로고    scopus 로고
    • Allosteric binding: Structures reveal new ways to tame G protein-coupled receptors
    • Cooke, R. & Congreve, M. Allosteric binding: structures reveal new ways to tame G protein-coupled receptors. Future Med. Chem. 8, 2007-2007 (2016).
    • (2016) Future Med. Chem , vol.8 , pp. 2007
    • Cooke, R.1    Congreve, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.