6QNK

Antibody FAB fragment targeting Gi protein heterotrimer

Summary for 6QNK

• Entry DOI: 10.2210/pdb6qnk/pdb
• Descriptor: FAB light chain, FAB heavy chain, TETRAETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: antibody fab fragment, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 4
• Total formula weight: 112812.87

Authors

Tsai, C.-J.,Muehle, J.,Pamula, F.,Dawson, R.J.P.,Maeda, S.,Deupi, X.,Schertler, G.F.X. (deposition date: 2019-02-11, release date: 2019-07-10, Last modification date: 2024-01-24)

Primary citation

Tsai, C.J.,Marino, J.,Adaixo, R.,Pamula, F.,Muehle, J.,Maeda, S.,Flock, T.,Taylor, N.M.,Mohammed, I.,Matile, H.,Dawson, R.J.,Deupi, X.,Stahlberg, H.,Schertler, G.
Cryo-EM structure of the rhodopsin-G alpha i-beta gamma complex reveals binding of the rhodopsin C-terminal tail to the G beta subunit.
Elife, 8:-, 2019

PubMed Abstract: One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway.

PubMed: 31251171
DOI: 10.7554/eLife.46041

Experimental method

X-RAY DIFFRACTION (1.9 Å)