Histamine acts by binding to specialized membrane proteins called histamine H1 receptors. These receptors, found in specific cells, are integral membrane proteins that possess seven transmembrane a-helical regions. The amino terminus of the protein is extracellular, while the C-terminus is cytoplasmic. The binding of histamine to the extracellular portion of the H1 receptor prompts a conformational change in the intracellular C-terminus region of the protein. This conformational change triggers numerous intracellular signaling events that stimulate the immune response in cells containing the receptor.There are numerous anti-histamine drugs available commercially. Some of the most popular are shown here side by side with histamine:- **Histamine Structure:** A simple organic compound, consisting of an imidazole ring with an ethylamine chain.- **Allegra (Fexofenadine) Structure:** A more complex structure featuring multiple ring systems, including a piperidine ring and a benzhydryl group, along with an ethyl ester and hydroxyl groups.- **Claritin (Loratadine) Structure:** Characterized by a tricyclic framework with a characteristic carbamate group and additional ethyl and chlorine substituents.**Prompt for Further Exploration:**Propose a reasonable mode of action by which these antihistamines exert their activity. Include relevant details about the system of your own choosing.

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The gene for a eukaryotic polypeptide 300 amino acid residues Iong is altered so that a signal sequence recognized by SRP occurs at the polypeptide's amino terminus and a nuclear localization signal (NLS) occurs internally, beginning at residue 150. Where is the protein likely to be found in the cell?
Some proteins may be phosphorylated by enzymes called kinases. Which of the following statements best describes this type of post-translational modification (PTM)? Phosphorylation is an irreversible modification of an amino acid side chain in the protein. Phosphorylation is a reversible modification of an amino acid side chain in the protein. Phosphorylation is an irreversible modification of the peptide backbone. Phosphorylation is a reversible modification of the peptide backbone.
Melanosomes are specialized lysosomes that storepigments for eventual release by exocytosis. Various cellssuch as skin and hair cells then take up the pigment, whichaccounts for their characteristic pigmentation. Mousemutants that have defective melanosomes often have paleor unusual coat colors. One such light-colored mouse, theMocha mouse (Figure Q13–3), has a defect in the gene forone of the subunits of the adaptor protein complex AP3,which is associated with coated vesicles budding from thetrans Golgi network. How might the loss of AP3 cause adefect in melanosomes?
The amino acid sequence Leu-His-Arg-Leu-Asp-Ala-Gln-SerLys-Leu-Ser-Ser is a signal sequence that directs proteinstowards the endoplasmic reticulum, say if it is true or false if it is false justify it.
I am studying pancreatic islet cells and have isolated, cloned, and sequenced a novel protein that you postulate has 4 transmembrane segments. What kind of experiment would allow me to test this hypothesis that there are 4 trans membrane segments?
Trans membrane proteins are co- translationally inserted into the ER membrane such that their cytoplasmic domains will be oriented within the ER lumen after translation is complete. true false
Which amino acids would you expect to find buried in the interior of peripheral membrane protein ?
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An integral membrane protein has an ER signal sequence near its N terminus and a stop transfer sequence in the middle. If a mutation removed the stop-transfer sequence, where would you expect to find the protein? Why?
Many of the proteins produced in the endoplasmic reticulum undergo modifications such as the addition of carbohydrates (oligosaccharides). What is the role of these sugars in such proteins?
The following figure shows the 3D structure of a tubulin dimer. A mutation in the beta tubulin subunit (shown in red) prevents the binding of a GTP molecule. Predict the consequences that this mutation will have on the microtubule and on cell division. Please be specific. Alpha tubulin Beta tubulin
A 160 residue polytopic integral plasma membrane protein has the following sequence at its N-terminus. The amino terminal Ser is located inside the cytoplasm. Amino acids 11- 14 are localized outside the cell. N-¹Ser-Tyr-Leu-Gln-Ile-Arg-Phe-Asn-Leu-Lys-11 Gly-Pro-Gly-Ser-15 Glu-Phe-Gln-Leu-Asp- Ile-His-Leu-23 Ser-Gly-Gly Carefully analyze the sequence. (a) What do you predict for the overall tertiary structure of the entire 160 residue protein? (b) Give at least three reasons for your prediction. Ruling out alternatives, with proper logic, can count as a reason.

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