Structure tridimensionnelle du récepteur de l’adénosine A2A lié à son agoniste naturel l’adénosine

Guillaume Lebon; Christopher G. Tate

doi:10.1051/medsci/20112711004

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Volume 27 / Numéro 11 (Novembre 2011)

Med Sci (Paris), 27 11 (2011) 926-928

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Numéro		Med Sci (Paris) Volume 27, Numéro 11, Novembre 2011


Page(s)		926 - 928
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/20112711004
Publié en ligne		30 novembre 2011

Gloriam DE, Fredriksson R, Schioth HB. The G protein-coupled receptor subset of the rat genome. BMC Genomics 2007 ; 8 : 338. [CrossRef] [PubMed] [Google Scholar]
Jacobson KA, Gao ZG. Adenosine receptors as therapeutic targets. Nat Rev Drug Discov 2006 ; 5 : 247–264. [CrossRef] [PubMed] [Google Scholar]
Yao XJ, Velez Ruiz G, Whorton MR, et al. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. Proc Natl Acad Sci USA 2009 ; 106 : 9501–9506. [CrossRef] [Google Scholar]
Cherezov V, Rosenbaum DM, Hanson MA, et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 2007 ; 318 : 1258–1265. [CrossRef] [PubMed] [Google Scholar]
Warne T, Serrano-Vega MJ, Baker JG, et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 2008 ; 454 : 486–491. [CrossRef] [PubMed] [Google Scholar]
Jaakola VP, Griffith MT, Hanson MA, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 2008 ; 322 : 1211–1217. [CrossRef] [PubMed] [Google Scholar]
Scheerer P, Park JH, Hildebrand PW, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 2008 ; 455 : 497–502. [CrossRef] [PubMed] [Google Scholar]
Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 2011 ; 469 : 175–180. [CrossRef] [PubMed] [Google Scholar]
Lebon G, Warne T, Edwards PC, et al. Agonist-bound adenosine A(2A) receptor structures reveal common features of GPCR activation. Nature 2011 ; 474 : 521–525. [CrossRef] [PubMed] [Google Scholar]
Lebon G, Bennett K, Jazayeri A, Tate CG. Thermostabilisation of an agonist-bound conformation of the human adenosine A(2A) receptor. J Mol Biol 2011 ; 409 : 298–310. [CrossRef] [PubMed] [Google Scholar]
Warne T, Moukhametzianov R, Baker JG, et al. The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor. Nature 2011 ; 469 : 241–244. [CrossRef] [PubMed] [Google Scholar]
Xu F, Wu H, Katritch V, et al. Structure of an agonist-bound human A2A adenosine receptor. Science 2011 ; 332 : 322–327. [CrossRef] [PubMed] [Google Scholar]
Chames P, Baty D. The future of antibody fragments, made of a single immunoglobulin domain. Med Sci (Paris) 2009 ; 25 : 1159–1162. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]

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[1] Gloriam DE, Fredriksson R, Schioth HB. The G protein-coupled receptor subset of the rat genome. BMC Genomics 2007 ; 8 : 338. [CrossRef] [PubMed] [Google Scholar]

[2] Jacobson KA, Gao ZG. Adenosine receptors as therapeutic targets. Nat Rev Drug Discov 2006 ; 5 : 247–264. [CrossRef] [PubMed] [Google Scholar]

[3] Yao XJ, Velez Ruiz G, Whorton MR, et al. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. Proc Natl Acad Sci USA 2009 ; 106 : 9501–9506. [CrossRef] [Google Scholar]

[4] Cherezov V, Rosenbaum DM, Hanson MA, et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 2007 ; 318 : 1258–1265. [CrossRef] [PubMed] [Google Scholar]

[5] Warne T, Serrano-Vega MJ, Baker JG, et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 2008 ; 454 : 486–491. [CrossRef] [PubMed] [Google Scholar]

[6] Jaakola VP, Griffith MT, Hanson MA, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 2008 ; 322 : 1211–1217. [CrossRef] [PubMed] [Google Scholar]

[7] Scheerer P, Park JH, Hildebrand PW, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 2008 ; 455 : 497–502. [CrossRef] [PubMed] [Google Scholar]

[8] Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 2011 ; 469 : 175–180. [CrossRef] [PubMed] [Google Scholar]

[9] Lebon G, Warne T, Edwards PC, et al. Agonist-bound adenosine A(2A) receptor structures reveal common features of GPCR activation. Nature 2011 ; 474 : 521–525. [CrossRef] [PubMed] [Google Scholar]

[10] Lebon G, Bennett K, Jazayeri A, Tate CG. Thermostabilisation of an agonist-bound conformation of the human adenosine A(2A) receptor. J Mol Biol 2011 ; 409 : 298–310. [CrossRef] [PubMed] [Google Scholar]

[11] Warne T, Moukhametzianov R, Baker JG, et al. The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor. Nature 2011 ; 469 : 241–244. [CrossRef] [PubMed] [Google Scholar]

[12] Xu F, Wu H, Katritch V, et al. Structure of an agonist-bound human A2A adenosine receptor. Science 2011 ; 332 : 322–327. [CrossRef] [PubMed] [Google Scholar]

[13] Chames P, Baty D. The future of antibody fragments, made of a single immunoglobulin domain. Med Sci (Paris) 2009 ; 25 : 1159–1162. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]