Solution
GPCR structure and function-
- GPCRs are integral
membrane proteins that possess seven membrane-spanning domains or
transmembrane helices. The extracellular parts of the receptor can
be glycosylated. These extracellular loops also contain two highly
conserved cysteine residues that form disulfide bonds to stabilize
the receptor structure.
G protein with activation-
- Heterotrimeric G-proteins are
composed of three distinct subunits (α, β, and γ).
- There are many different α, β, and
γ subunits, allowing a bewildering number of G-protein
permutations.
- Regardless of the specific
composition of the heterotrimeric G-protein, its α subunit binds to
guanine nucleotides, either GTP or GDP.
- Binding of GDP allows the α subunit
to bind to the β and γ subunits to form an inactive trimer. Binding
of an extracellular signal to a G-protein-coupled receptor allows
the G-protein to bind to the receptor and causes GDP to be replaced
with GTP (Figure 8.5A). When GTP is bound to the G-protein, the α
subunit dissociates from the βγ complex and activates the
G-protein.
- Following activation, both the
GTP-bound α subunit and the free βγ complex can bind to downstream
effector molecules and mediate a variety of responses in the target
cell