Question 2 You are using molecular modelling software to examine the X-ray crystal structure of the B2-adrenoceptor. You have access to two quality structural images of: a B2-adrenoceptor bound to a full agonist (BI-167107), and a B2-adrenoceptor bound to an inverse agonist (carazolol). You would like to understand the nature and magnitude of the conformational changes made by the B2-adrenoceptor as it moves from an inactive to active state. Question 2a What regions of the receptor would you expect to show the largest conformational changes? Provide a rationale for your answer. Question 2b Describe how you could use information from the two X-ray crystal structures to determine what the conformational changes are. G protein-coupled receptors, such as the B2-adrenoceptor, normally only have a single C-terminus end and a single N-terminus end. However, when examining the X-ray crystal structure of the B2- adrenoceptor bound to the inverse agonist, there appear to be parts of the B2-adrenoceptor structure that are not visible, as evidenced by the multiple protein "ends" (highlighted by the black arrows in Figure 1 below). Figure 1. Question 2c. What is the likely reason for the missing segments of the protein?
Question 2 You are using molecular modelling software to examine the X-ray crystal structure of the B2-adrenoceptor. You have access to two quality structural images of: a B2-adrenoceptor bound to a full agonist (BI-167107), and a B2-adrenoceptor bound to an inverse agonist (carazolol). You would like to understand the nature and magnitude of the conformational changes made by the B2-adrenoceptor as it moves from an inactive to active state. Question 2a What regions of the receptor would you expect to show the largest conformational changes? Provide a rationale for your answer. Question 2b Describe how you could use information from the two X-ray crystal structures to determine what the conformational changes are. G protein-coupled receptors, such as the B2-adrenoceptor, normally only have a single C-terminus end and a single N-terminus end. However, when examining the X-ray crystal structure of the B2- adrenoceptor bound to the inverse agonist, there appear to be parts of the B2-adrenoceptor structure that are not visible, as evidenced by the multiple protein "ends" (highlighted by the black arrows in Figure 1 below). Figure 1. Question 2c. What is the likely reason for the missing segments of the protein?
Chapter27: Medications That Affect The Nervous System
Section: Chapter Questions
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Transcribed Image Text:Question 2
You are using molecular modelling software to examine the X-ray crystal structure of the
B2-adrenoceptor. You have access to two quality structural images of:
a B2-adrenoceptor bound to a full agonist (BI-167107), and
a B2-adrenoceptor bound to an inverse agonist (carazolol).
You would like to understand the nature and magnitude of the conformational changes made by the
B2-adrenoceptor as it moves from an inactive to active state.
Question 2a
What regions of the receptor would you expect to show the largest conformational changes?
Provide a rationale for your answer.
Question 2b
Describe how you could use information from the two X-ray crystal structures to determine what the
conformational changes are.
G protein-coupled receptors, such as the B2-adrenoceptor, normally only have a single C-terminus
end and a single N-terminus end. However, when examining the X-ray crystal structure of the B2-
adrenoceptor bound to the inverse agonist, there appear to be parts of the B2-adrenoceptor
structure that are not visible, as evidenced by the multiple protein "ends" (highlighted by the black
arrows in Figure 1 below).
Figure 1.
Question 2c.
What is the likely reason for the missing segments of the protein?
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