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NMR backbone and methyl resonance assignments of an inhibitory G-alpha subunit in complex with GDP.

Biomol. NMR Assign. 13, 131-137 (2019)
Postprint DOI Verlagsversion bestellen
Open Access Green
G-proteins are essential switch points at the cell membrane that control downstream signaling by their ability to adopt an inactive, GDP-bound or an active, GTP-bound state. Among other exchange factors, G-protein coupled receptors (GPCRs) induce exchange of GDP to GTP and thus promote the active state of the G-protein. The nucleotide-binding subunit of the G-protein undergoes major conformational changes upon nucleotide binding. Thus, an NMR analysis of the two distinct nucleotide-bound states is essential for a more detailed understanding of associated structural changes. Here, we provide an NMR backbone as well as methyl group resonance assignment of an inhibitory G-alpha subunit subtype 1 (G(i,1)) in the GDP-bound form and show that, in contrast to the GTP-bound form, large parts of the protein are mobile, presumably caused by a loose arrangement of the two subdomains in G that tightly interact with each other only in the GTP-bound state. As the GDP-bound form represents the GPCR-binding-competent state, the presented NMR data will be essential for further studies on G-protein-GPCR interactions and dynamics in solution for receptor systems that couple to G-proteins containing an inhibitory G,1 subunit.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Gpcr ; G-protein ; Nucleotide Binding ; Nmr ; Signal Transduction; G-protein; Crystal-structure; Receptor; Activation; Reconstruction
ISSN (print) / ISBN 1874-2718
e-ISSN 1874-270X
Quellenangaben Band: 13, Heft: 1, Seiten: 131-137 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands
Begutachtungsstatus Peer reviewed