You perform a competition study on a GPCR. You have isolated the plasma membrane from cells which contains the GPCR of interest. If an agonist and an inverse agonist are at equal concentrations in your study but the inverse agonist has a 10 x higher affinity for the receptor than the agonist, what would you expect to be the overall outcome to be? More of the agonist is bound and so most of the receptor is in its active conformation and is stimulated More of the inverse agonist is bound and so most of the receptor is in its inactive conformation and is unstimulated.

You perform a competition study on a GPCR. You have isolated the plasma membrane from cells which contains the GPCR of interest. If an agonist and an inverse agonist are at equal concentrations in your study but the inverse agonist has a 10 x higher affinity for the receptor than the agonist, what would you expect to be the overall outcome to be? More of the agonist is bound and so most of the receptor is in its active conformation and is stimulated More of the inverse agonist is bound and so most of the receptor is in its inactive conformation and is unstimulated.

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter6: Cell Communication

Section6.3: Reception

Problem 2C

See similar textbooks

Similar questions

Estimate the binding affi nity of a ligand for its receptor from the followingdata:
A ligand binds two different receptors with a Kd value of 10−7 M for receptor 1 and a Kd value of 10−9 M for receptor 2. For which receptor does the ligand show the greater affinity? Calculate the fraction of receptors that have a bound ligand ([RL]/RT) in the case of receptor 1 and receptor 2 if the con- centration of free ligand is 10−8 M.
α-Bungarotoxin is a powerful neurotoxin found in the venom of a poisonous snake (Bungarus multicinctus). It binds with high specificity to the acetylcholine receptor (AChR; an integral membrane protein) andprevents its ion channel from opening. This interaction was used to purify AChR from the electric organ of torpedo fish.(a) Outline a strategy for using α-bungarotoxin covalently bound to chromatography beads to purify the AChR protein. (b) Outline a strategy for the use of [125I]α-bungarotoxin to purify the AChR protein.
3) Acetylcholine binds to a GPCR on heart muscle, making the heart beat more slowly. The activated receptor stimulates a G protein, which opens a K+ channel in the plasma membrane, as shown in Figure 1. Which of the following would enhance this effect of the acetylcholine? (a) (b) (c) (d) Figure 1 addition of a high concentration of a non-hydrolyzable analog of GTP addition of a drug that prevents the a subunit from exchanging GDP for GTP mutations in the acetylcholine receptor that weaken the interaction between the receptor and acetylcholine mutations in the acetylcholine receptor that weaken the interaction between the receptor and the G protein
An analog of cGMP, 8-Br-cGMP, will permeate cellular membranes, is only slowly degraded by a rod cell’s PDE activity, and is as effective as cGMP in opening the gated channel in the cell’s outer segment. If you suspended rod cells in a buffer containing a relatively high [8-Br-cGMP], then illuminatedthe cells while measuring their membrane potential, what would you observe?
Of membrane-bound receptors and nuclear receptors, which is betteradapted for mediating a response that lasts a considerable length oftime, and which is better for mediating a response with a rapid onset andshort duration? Explain why.
Do you consider GPCR is intracellular or membrane bound receptor?? Explain it
Name three features common to the activation of cytokine receptors and receptor tyrosine kinases. Name one difference with respect to the enzyme activity of these receptors.
How can you decrease (or stop) the rate of binding for a noncompetitive inhibitor? Could you change the receptor allosteric sites to prevent noncompetitive binding?
added ligand concentration of 10 µM is 5 × 10³ s¹. What is the value of the reverse rate constant k_1 = 1 ×10-4 Incorrect Macmillan Learning You have not correctly calculated the value of the reverse rate constant. To begin, calculate the value of k₁ by dividing the rate of receptor-ligand complex formation (the rate of the forward reaction) by the ligand concentration. k₁ = rate forward [L] Then, calculate the value of the reverse rate constant, k_₁, by multiplying the dissociation constant, Kd, and the forward rate constant, k₁. k_1 = Kak₁
D Question 18 Which of the following statements describes the signal amplification that results from activation of the G-protein coupled receptor? Fragmentation of the G-protein leads to an increase in entropy O The binding of a ligand to the receptor increases the chances of the receptor binding a G-protein The binding of a G-protein to the receptor increases the chances of it exchanging GDP for GTP O The ligand is bound to the receptor sufficiently long such that the receptor can fragment several G-proteins
From the Hill Plot below, the of the first binding event for the receptor-ligand system under study is: Q1 4nM Ο 10 μΜ -2 nM 2 nM Calculate the Hill Coefficient from the receptor-ligand binding data below: Q2 4 100 2 3 (0-1) 60 log 10 8 6 4 2 0 -2 -4 -6 -6 -4 -2 0 2 4 log [L] (nM) 6 8 10