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, has the highest specificity in binding to the target Protein J?
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- Cyclic adenosine monophosphate (CAMP) is a molecule that can act as anallosteric activator of kinase enzymes inside of the cytoplasm. Describehow CAMP molecules affect kinase enzymes?Signal-transducing heterotrimeric G proteins consist of three subunits designated α, β, and γ. The Gα subunit is a GTPase switch protein that cycles between active and inactive states depending on whether it is bound to GTP or to GDP. Review the steps for ligand-induced activation of effector proteins mediated by the heterotrimeric G proteins. Suppose that you have isolated a mutant Gα subunit that has an increased GTPase activity. What effect would this mutation have on the G protein and the effector protein?Between direct and indirect allosteric kinase inhibitors, which do you think requires a larger conformational change in response to binding of the allosteric modulator? Why?
- Briefly describe the following properties of the Rab and Arf GTPases: a) Size, structure and cellular localization (for structure I want to know if they are lipidated and any other unique features) , b) How are they activated and inactivated (i.e. include the GEFs and GAPs), c). Give an example of downstream cellular effects.For the protein Calmodulin-1: 1) this protein have any secondary, tertiary and/or quaternary structures present? 2) Are there any molecular additions to this protein that are not amino acids?For both questions, can you explain if so, where specifically? The protein Calmodulin-1 is stated to have the molecular function of signaling receptor binding which is interrelated with the biological function of calcium-mediated signaling. Can you explain this relationship?What is the purpose of A kinase–associated proteins (AKAPs)? Describe how AKAPs work in heart muscle cells.
- Continuous exposure of a Gαs protein coupled receptor to its ligand leads to a phenomenon known as desensitization. Describe several molecular mechanisms for receptor desensitization. How can a receptor be reset to its original sensitized state? What effect would a mutant receptor lacking serine or threonine phosphorylation sites have on a cell?If you have a protein kinase that is regulated by both small molecule inhibitors as well as by phosphorylation, and is part of a cooperative enzyme complex that works as part of a larger pathway involving kinase and GTPase proteins please explain where on this protein regulation could occur, how different types of inhibition could control the function of the protein as well as the function of the complex, and how the protein could regulate other proteins. (This question was previously answered but it was answered incompletely mentioning an herbicide developed in the 1950's. Apparently, it was a plagiarized excerpt from an NCBI article. This is a repost for a full and complete answer. Thank you so much for your help! :) )An SH2-containing protein contains a mutation that changes its binding pocket such that tyrosine and phosphotyrosine bind with equal affinity. As a result, MEK activity: does not change with receptor dimerization and transautophosphorylation decreases due to changes in Raf activation increases with ligand binding-induced dimerization decreases due to allosteric inhibition of SH2-domain binding
- Pathway analysis: Link the protein names to the correct statements by interrogating the depicted pathway. Options: A. RTK Receptor Threonine Kinase B. GEF Guanidine Exchange Factor C. PLC Phospholipase C D. GAP GTPase Activating Protein E. Gαi F. Raf Rapidly Accelerated Fibrosarcoma G. PAK1 p21 Activated Kinase H. WASP Wiscott Aldrich syndrome protein I. RTK Receptor Tyrosine Kinase J. GPCR G-protein Coupled Receptor K. Steroid Receptor L. Phosphatase M. MEK1 (Mitogen-Activated Protein) Kinase/ERK (Extracellular Signal-Regulated Kinase) Kinase 1 N. AC Adenylyl cyclase O. IP3R IP3 Receptor P. ERK1/2 Extracellular Signal-Regulated KinaseContinuous exposure of a G protein-coupled receptor to its ligand leads to a phenomenon known as desensitization. Describe several molecule mechanisms for receptor desensitizationI just read an abstract of the paper “Disulfide bond-disrupting agents activate the tumor necrosis family-related apoptosis-inducing ligand/death receptor 5 pathway” and noted that “DDAs and TRAIL synergize to kill cancer cells and are cytotoxic to HER2+ cancer cells with acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib.” For the last sentence, I am not sure the meaning of the “acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib”. Is the “acquired resistance ... to inhibitor” a good thing or bad thing, as far as the synergize effect of DDAs and TRAIL”? Hope that expert can help.