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MO29 GPCRs

Mer Scott 6 questions

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  1. 1We can study how GPCR shape changes by a) comparing [blank_start]crystal structures[blank_end] in different ‘frozen’
    states across the [blank_start]same[blank_end] GPCR and b) running dynamic [blank_start]computer simulations[blank_end] of GPCRs and
    ligand [blank_start]binding[blank_end] events.
    1. Acrystal structures
    2. Bsame
    3. Ccomputer simulations
    4. Dbinding
  2. 2GPCRs contain 7 [blank_start]alpha helices[blank_end] and cluster together in [blank_start]different[blank_end] conformations to change the [blank_start]activity[blank_end] of the GPCR. Networks of hydrogen bonds, ionic bonds, and hydrophobic interactions can '[blank_start]pause[blank_end]' the structure dynamics.
    1. Aalpha helices
    2. Bdifferent
    3. Cactivity
    4. Dpause
  3. 3Choose the incorrect statement about ligand binding to GPCRs.
    1. AAgonist binding stabilises ‘active’ conformations
    2. BAgonist binding at one side of receptor changes receptor conformation at other end
    3. CPart of the reason for differences in efficacy and potency between different agonists is stabilisation of a slightly different GPCR conformation
    4. DInverse agonist binding stabilises ‘inactive’ conformations
    5. EA stabilised conformation is no longer dynamic
  4. 4Choose the best description of an allosteric ligand.
    1. AA ligand that binds to a different receptor location to the ‘pocket’ that the endogenous agonist binds to
    2. BA ligand that changes the conformational shape of the GPCR (induced fit)
    3. CA ligand that binds to the same receptor location that the endogenous agonist binds to
  5. 5Order the steps from binding to a GPCR to cellular action being taken.

    [blank_start]2[blank_end]. Receptor undergoes conformational change which is transmitted to the cytosolic regions
    [blank_start]5[blank_end]. Activated α and β-γ complex bind to and activate target proteins
    [blank_start]6[blank_end]. Signalling cascade of downstream targets occurs
    [blank_start]3[blank_end]. Trimeric GDP binding protein is activated; α and γ subunits are covalently attached to the phospholipid bilayer, third subunit is β
    [blank_start]1[blank_end]. Protein ligand binds
    [blank_start]4[blank_end]. α subunit changes shape, exchanges GDP for GTP
    1. A2
    2. B5
    3. C6
    4. D3
    5. E1
    6. F4
  6. 6Historically when named, GPCRs were thought to couple [blank_start]obly[blank_end] to G proteins. More recently [blank_start]β-arrestin[blank_end] was discovered as able to couple to GPCRs. It has mixed function, it a) solely [blank_start]blocks[blank_end] G protein binding or b) it can [blank_start]facilitate[blank_end] G protein independent signalling pathways.
    1. Aonly
    2. Bβ-arrestin
    3. Cblocks
    4. Dfacilitate

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Description
PHCY211 (Molecules) Quiz on MO29 GPCRs, created by Mer Scott on 15/04/2018.
Author
Mer Scott
Language
English
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