Concept explainers
To determine: What would be the difficulties of finding cancer drugs that works by inhibiting tyrosine kinase given that similar kinases also function in normal cells.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
To suggest: Whether it could be possible to develop such new medication through government-sponsored research. Why or why not.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
To suggest: Alternatives if it is not possible to develop new such medication through government-sponsored research.
Introduction: Enzyme-linked receptor is a transmembrane protein with a binding site for signaling molecule outside the cell and an enzyme component inside the cell. An example of enzyme-linked receptor is tyrosine kinase. On binding of ligands with the enzyme-linked receptors, receptor protein comes close together in the plasma membrane and forms dimer which initiates activation of downstream molecules and causes cellular response.
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Biology (MindTap Course List)
- When a signal binds to the Tyrosine kinase receptor (RTK), you have studied that a list of events occur sequentially. Map the events in the correct order from 1st to the last step.arrow_forwardWhat is the purpose of A kinase–associated proteins (AKAPs)? Describe how AKAPs work in heart muscle cells.arrow_forwardOf the steps listed below, which problem would take you the longest to realize you had a problem in your RTK (ie the highest number of earlier steps could still occur)? O the RTK cannot autophosphorylate O the RTK cannot phosphorylate downstream kinases the RTK cannot integrate into the membrane the extracellular ligand cannot bind to the RTKarrow_forward
- Rous Sarcoma Virus can cause cancer in infected cells. The tumor causing nature of the virus is linked to it harbouring a gene that codes for a unique receptor tyrasine kinase (RTK). What is it about the tyrosine kinase that accounts for the tumor-causing nature of the virus? O It is unrelated to any human kinase and thus is able to act uncontrollably in causing cell division. O It cantain activate downstream effectors without binding to a SH2 domain. O It lacks the carboxy-terminal regulatory domain that is present in RTKS of non-cancerous cells.arrow_forwardHow could we promote rapid or slow signaling for medical purposes? So there are many examples of slow and rapid signaling via coupled receptors. For an example, salivary gland secretion is rapid signaling and cell growth is slow signaling. These pathways could be twisted and used to resolve medical issues in a more natural and less damaging way. Are there any experiments that have or could be done to test out promoting rapid signaling to speed up slow processes such as cell growth in a severe wound? What experiments have or could be done to test out slowing down signaling that is fast like cells responding to their environment negatively (over-active allergies)? Thank you.arrow_forwardPay close attention to the information related to figure 3.14a and the structure of the PKA catalytic site in this figure. In a few well-written sentences, propose the following: A mutation that would result in PKA becoming a dead kinase*. A mutation that would result in PKA becoming a constitutively active** kinase.arrow_forward
- a) b) You walk into university and see that everyone has become a unicorn. You try to hide in bluezone only to figure out that everyone can sense you. You are kidnapped by a unicorn, and they ask you: "How do kinases work?" You wake up realizing it was all a dream, but you still wonder: how do kinases work? Hydrolyze the protein and then ATP to activate it First hydrolyze ATP and then transfer Pi to activate a protein Tranfer a free Pi and then hydrolyze ATP to make more free Pi Bind GTP after releasing GDP from the alpha subunitarrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, has the highest specificity in binding to the target Protein J?arrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: Describe the relative binding affinities of Ligand A to Protein K and to the active and inactive forms of Protein J. Determine which will Ligand A bind with the highest, medium, and lowest affinity.arrow_forward
- Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, may be expected to be the most potent or have the highest activity against cancer? Explain. b. Which of the ligands, based on the table, may be expected to be least toxic to normal cells? Explain.arrow_forwardCyclin-dependent kinases are a type of "microchip" protein that require multiple inputs (i.e., structural alterations) to be activated-- and thus are active only under specific conditions (as shown in the diagram below). How does limiting activity to when all conditions have been met help the cell function properly? INPUTS has this phosphate been removed? been added? has this is cyclin present? phosphatearrow_forwardNeed helparrow_forward
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning