5 Questions
Which part of the G protein-coupled receptor forms ligand-binding pockets?
Loops on the extracellular side
What contributes to the unusually stable structure of rhodopsin?
Its permanently bound ligand
What happens when a ligand binds to an inactive GPCR?
It disturbs noncovalent interactions
What happens when an active GPCR forms a complex with a G protein?
It induces a conformational change in the α subunit of the G protein
How many G protein molecules can a single receptor activate for signal amplification?
Several
Study Notes
- G protein-coupled receptors have a specific topology.
- Ligand-binding pockets are formed by three loops on the outside of the cell.
- Three loops on the cytoplasmic side provide binding sites for signaling proteins.
- Rhodopsin has an unusually stable structure due to its permanently bound ligand.
- Several GPCR crystal structures have been discovered since 2007.
- Ligand binding disturbs noncovalent interactions in the inactive conformation.
- This causes the receptor to assume an active conformation.
- The active receptor forms a complex with a G protein.
- The interaction induces a conformational change in the α subunit of the G protein.
- A single receptor can activate multiple G protein molecules for signal amplification.
"Unlock the Secrets of G Protein-Coupled Receptors: Test Your Knowledge Now!" Explore the fascinating world of G protein-coupled receptors (GPCRs) with this quiz. From their unique topology to ligand-binding pockets, discover key insights into these important signaling molecules. Brush up on the latest research, including the discovery of several GPCR crystal structures since 2007. Test your understanding of how ligand binding induces conformational changes and activates signaling pathways. Don't miss this chance
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