Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity.
- Resource Type
- Article
- Authors
- Ching-Ju Tsai; Pamula, Filip; Nehmé, Rony; Mühle, Jonas; Weinert, Tobias; Flock, Tilman; Nogly, Przemyslaw; Edwards, Patricia C.; Carpenter, Byron; Gruhl, Thomas; Pikyee Ma; Deupi, Xavier; Standfuss, Jörg; Tate, Christopher G.; Schertler, Gebhard F. X.
- Source
- Science Advances. Sep2018, Vol. 4 Issue 9, p1-9. 9p.
- Subject
- *G protein coupled receptors
*RHODOPSIN
*CRYSTAL structure
*C-terminal residues
*ANGIOTENSIN receptors
- Language
- ISSN
- 2375-2548
The article focuses on a research which report the crystal structure of light-sensitive G protein coupled receptors (GPCRs) rhodopsin bound to an engineered mini-G protein. It mentions rhodopsin seems to adopt predominantly one thermodynamically stable active conformation and analysis of the well-defined GPCR–G protein interface suggests that the precise position of the carboxyl-terminal. It also mentions receptor is a significant determinant in selective G protein activation.