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A protein’s function depends on its specific conformation
A protein’s function depends on its specific conformation

... • In almost every case, the function depends on its ability to recognize and bind to some other molecule. – For example, antibodies bind to particular foreign substances that fit their binding sites. – Enzyme recognize and bind to specific substrates, facilitating a chemical reaction. – Neurotransmi ...
Signal Transduction
Signal Transduction

... Only signal molecules able to cross the plasma membrane (e.g., steroid hormones) interact with intracellular receptors. A large family of cell surface receptors have a common structural motif, 7 transmembrane a-helices. Rhodopsin was the first of these to have its 7-helix structure confirmed by X-ra ...
sc-PDB: an annotated database of druggable binding sites from the
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... [1] Kellenberger, E., Muller, P., Schalon, C., Bret, G., Foata, N. and Rognan, D. (2006). sc-PDB: an Annotated Database of Druggable Binding Sites from the Protein Data Bank J. chem. Inf. Model. 46, 717-727. [2] Surgand, J.-S.; Rodrigo, J.; Kellenberger, E. and Rognan, D. (2006). A chemogenomic anal ...
Cellular Communication
Cellular Communication

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Cell Signaling Website Slides_10_4_11
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SECOND MESSANGERS - MBBS Students Club
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... transmembrane proteins that physically interact with a complex containing a GTPase, called a heterotrimeric G protein. These polytopic membrane proteins are collectively termed G-protein-coupled receptors (GPCRs) and their ligands are as diverse as is the GPCR family itself. Rhodopsin is a familiar ...
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G-Protein Coupled Signal Transduction

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Enzyme Regulation - University of San Diego Home Pages
Enzyme Regulation - University of San Diego Home Pages

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Lecture 12
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Technical data sheet
Technical data sheet

... Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested use of this reagent is 0.5 - 4.0 µg per ml. It is recommended that the reagent be titrated for optimal performance for each application. ...
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G protein–coupled receptor



G protein–coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein–coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. Two of the United States's top five selling drugs (Hydrocodone and Lisinopril) act by targeting a G protein–coupled receptor. The 2012 Nobel Prize in Chemistry was awarded to Brian Kobilka and Robert Lefkowitz for their work that was ""crucial for understanding how G protein–coupled receptors function."". There have been at least seven other Nobel Prizes awarded for some aspect of G protein–mediated signaling.There are two principal signal transduction pathways involving the G protein–coupled receptors: the cAMP signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein's α subunit, together with the bound GTP, can then dissociate from the β and γ subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the α subunit type (Gαs, Gαi/o, Gαq/11, Gα12/13).
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