Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Montana State University, Bozeman, United States
2. Center for Biomolecular Structure and Dynamics, The University of Montana, Missoula, United States
Abstract
Funder
M.J. Murdock Charitable Trust
National Institutes of Health
Publisher
eLife Sciences Publications, Ltd
Subject
General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience
Link
https://cdn.elifesciences.org/articles/19238/elife-19238-v1.pdf
Reference60 articles.
1. The receptor-bound "empty pocket" state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic;Abdulaev;Biochemistry,2006
2. RIC-8 is required for GPR-1/2-dependent Galpha function during asymmetric division of C. elegans embryos;Afshar;Cell,2004
3. Activators of G protein signaling exhibit broad functionality and define a distinct core signaling triad;Blumer;Molecular Pharmacology,2014
4. Toward high-resolution de novo structure prediction for small proteins;Bradley;Science,2005
5. Molecular chaperoning function of Ric-8 is to fold nascent heterotrimeric G protein α subunits;Chan;PNAS,2013
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