, Ce modèle se base sur trois structures cristallographiques différentes (Figure 45), Prédiction des interactions RCPG:RCPG dans l'équipe, vol.3, p.2

[. Rasmussen, été utilisé pour modéliser l'interface RCPG:pG. La structure, 2011.

, a été ensuite utilisée pour créer l'interface entre deux complexes ?2AR:Gs. En procédant ainsi, l'ouverture en deux de la sous-unité ? de la protéine-G telle que décrite dans la structure du complexe ?2AR:Gs conduit à des clashes stériques importants entre les deux sous-unités ?

, le mode de dimérisation connu pour CXCR4 permet une imbrication parfaite des deux protéines-G. Ces assemblages faisant intervenir plusieurs protéines-G ont par ailleurs été proposés dans la littérature, En revanche, lorsqu'on utilise une structure inactive de la protéine-G hétéro-trimérique telle que Gi (code PDB : 1GP2), résolue à, p.3

. Cordomí, , 2015.

. Toutefois, aucun de ces modèles ne montre d'interactions protéine-G:protéine-G aussi complémentaires que dans notre modèle

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