Abstract
Dancing in the dark: Much is known about the structure and light-induced conformational changes of the mammalian dimlight receptor rhodopsin, a model system for the entire G-protein-coupled receptor family. Less attention has been paid to the dynamic properties of rhodopsin. Growing evidence for the presence of large backbone motions in the inactive dark-state conformation of rhodopsin and their importance for the functional, light-induced conformational changes necessary for signal transduction are reviewed here. Cysteine mutagenesis experiments and spectroscopic techniques are combined to reveal more information about the protein dynamics.
Original language | English (US) |
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Pages (from-to) | 981-986 |
Number of pages | 6 |
Journal | ChemBioChem |
Volume | 3 |
Issue number | 10 |
DOIs | |
State | Published - Oct 4 2002 |
Externally published | Yes |
Keywords
- Activation mechanism
- Conformation analysis
- G-protein-coupled receptors
- Helical structures
- Membrane proteins
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Organic Chemistry