Study questions Receptors 2023-03-23

1) How were receptors initially (historically) classified?

2) What are the three classes of surface receptors based on the principal signal transduction
mechanisms?
3) Give two examples of bacterial protein that have contributed to the structural understanding of
the eukaryotic pLGICs like the nAChRs?
4) What is the topology and function of these bacterial homologs?
5) Why is the neurotransmitter-binding site only formed at one of the interfaces between β2-α4
and not at the other interfaces between the subunits of the human α4β2 nicotinic receptor?
6) There are more than 800 GPCRs in man but only 15 Gα-subunits of the heterotrimeric G protein.
How does that effect the evolution of the GPCRs and the Gαs?
7) What is the definition of a GPCR? Is it a structural of functional definition? Is bacteriorhodopsin
a GPCR?
8) What is the function of bacteriorhodopsin? Do the solved structures originate from a
bacterium?
9) Explain the order of events in the functional mechanism of proton pumping in
bacteriorhodopsin.
10) Compare rhodopsin (e.g. from cow) and bacteriorhodopsin, what similarities are there?
11) To solve a structure of a protein it is necessary to have large amounts of the pure protein. Most
eukaryotic receptors are naturally only expressed at very low levels. Give two exceptions which
were exploited to generate structural information of receptors.
12) What is opsin?
13) What happens when rhodopsin is activated? How is light converted into an GEF activity?
14) Artificial constructs and techniques have been used to generate structural information. How can
we be sure that the information is physiological relevant?
15) Outline the structural rearrangements that occur when a GPCR bind a Gα.
16) Why is it difficult to obtain structural information of a protein complex from the free protein
structures?
17) What is optogenetics? Explain the concept of OptoXRs.
18) In what aspect is insulin binding to the insulin receptor similar to GPCR binding to a Gα?