Abstract
The G protein-coupled receptor (GPCR) signaling pathways mediating information exchange across the cell membrane are central to a variety of biological processes and therapeutic strategies, but visualizing the molecular-level details of this exchange has been difficult for all but a few GPCR-G protein complexes. A study by Gao et al. now reports new strategies and tools to obtain receptor complexes in a near-native state, revealing insights into the gross conformational features of rhodopsin-transducin interactions and setting the stage for future studies.
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication types
-
Research Support, N.I.H., Extramural
MeSH terms
-
Animals
-
Eye Proteins / chemistry
-
Eye Proteins / metabolism*
-
GTP-Binding Protein beta Subunits / chemistry
-
GTP-Binding Protein beta Subunits / metabolism*
-
GTP-Binding Protein gamma Subunits / chemistry
-
GTP-Binding Protein gamma Subunits / metabolism*
-
Humans
-
Models, Molecular*
-
Protein Interaction Domains and Motifs / radiation effects
-
Protein Multimerization / radiation effects
-
Rhodopsin / chemistry
-
Rhodopsin / metabolism*
-
Rod Cell Outer Segment / enzymology
-
Rod Cell Outer Segment / metabolism
-
Rod Cell Outer Segment / radiation effects
-
Transducin / chemistry
-
Transducin / metabolism*
Substances
-
Eye Proteins
-
GTP-Binding Protein beta Subunits
-
GTP-Binding Protein gamma Subunits
-
Rhodopsin
-
Transducin