Structural flexibility of the Gαs α-helical domain in the β2-adrenoceptor Gs complex

The active-state complex between an agonist-bound receptor and a guanine nucleotide-free G protein represents the fundamental signaling assembly for the majority of hormone and neurotransmitter signaling. We applied single-particle electron microscopy (EM) analysis to examine the architecture of ago...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2011-09, Vol.108 (38), p.16086-16091
Hauptverfasser:	Westfield, Gerwin H, Rasmussen, Søren G. F, Su, Min, Dutta, Somnath, DeVree, Brian T, Chung, Ka Young, Calinski, Diane, Velez-Ruiz, Gisselle, Oleskie, Austin N, Pardon, Els, Chae, Pil Seok, Liu, Tong, Li, Sheng, Woods, Virgil L. Jr, Steyaert, Jan, Kobilka, Brian K, Sunahara, Roger K, Skiniotis, Georgios
Format:	Artikel
Sprache:	eng
Schlagworte:	adrenergic receptors Architecture beta-adrenergic agonists Biological Sciences Crystal structure Electron microscopy Erythema multiforme G-proteins Gas density Gross domestic product guanosine diphosphate Micelles molecular models Nucleotides Particle density protein secondary structure Receptors
Online-Zugang:	Volltext
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