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Questions and Answers
Which part of the G protein-coupled receptor forms ligand-binding pockets?
Which part of the G protein-coupled receptor forms ligand-binding pockets?
- Loops on the extracellular side (correct)
- Helices on the cytoplasmic side
- Helices on the extracellular side
- Loops on the cytoplasmic side
What contributes to the unusually stable structure of rhodopsin?
What contributes to the unusually stable structure of rhodopsin?
- Its interaction with G protein
- Its extracellular loops
- Its permanently bound ligand (correct)
- Its cytoplasmic loops
What happens when a ligand binds to an inactive GPCR?
What happens when a ligand binds to an inactive GPCR?
- It stabilizes noncovalent interactions
- It activates the G protein
- It disturbs noncovalent interactions (correct)
- It induces a conformational change in the β subunit
What happens when an active GPCR forms a complex with a G protein?
What happens when an active GPCR forms a complex with a G protein?
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How many G protein molecules can a single receptor activate for signal amplification?
How many G protein molecules can a single receptor activate for signal amplification?
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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.
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