Sandbox reserved 1169: Difference between revisions
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=== Overall Structure === | === Overall Structure === | ||
[[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane ]] | [[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane ]] | ||
Like other G protein-coupled receptors, the neurotensin receptor is composed of 3 distinct regions. An extracellular binding site where neurotensin binds and causes a conformational change of the protein | Like other G protein-coupled receptors, the neurotensin receptor is composed of 3 distinct regions. An extracellular binding site where neurotensin binds and causes a conformational change of the protein. A region containing <scene name='72/727765/Overall_structure/1'>7 transmembrane alpha helices</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] that transduce the signal from the extracellular side of the cell membrane to the intracellular side. Lastly, an intracellular region that when activated by a conformational change in the protein activates a [https://en.wikipedia.org/wiki/G_protein G protein] associated with this receptor. Currently no crystal structures of the inactive form of the neurotensin receptor available. Without a representation of the inactive form, the conformational changes caused by agonist binding are still not completely known. | ||
=== Neurotensin Binding Site === | === Neurotensin Binding Site === | ||
Binding of NTS to the binding site is enriched by <scene name='72/721539/Binding_pocket_surface/3'>charge complementarity</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)]between the positive NTS arginine side chains and the [https://en.wikipedia.org/wiki/Electronegativity electronegative] pocket. In addition, the C-terminus forms a <scene name='72/721539/Binding_site_charges/2'>salt bridge</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] with R328. Only three out of eight [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bonds] are made between the side chains of NTS and the receptor. Most of the interactions are [https://en.wikipedia.org/wiki/Van_der_Waals_force van der Waals] interactions. The binding pocket is partially capped by a [https://en.wikipedia.org/wiki/Beta_hairpin β-hairpin loop] at the proximal end of the receptor protein's N-terminus.<ref name="White"/> | Binding of NTS to the binding site is enriched by <scene name='72/721539/Binding_pocket_surface/3'>charge complementarity</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)]between the positive NTS arginine side chains and the [https://en.wikipedia.org/wiki/Electronegativity electronegative] pocket. In addition, the C-terminus forms a <scene name='72/721539/Binding_site_charges/2'>salt bridge</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] with R328. Only three out of eight [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bonds] are made between the side chains of NTS and the receptor. Most of the interactions are [https://en.wikipedia.org/wiki/Van_der_Waals_force van der Waals] interactions. The binding pocket is partially capped by a [https://en.wikipedia.org/wiki/Beta_hairpin β-hairpin loop] at the proximal end of the receptor protein's N-terminus.<ref name="White"/> | ||
