Sandbox reserved 1169: Difference between revisions

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== Structure ==

=== Overall Structure ===

[[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane. This image depicts the spanning of the membrane made by NTSR1 and illustrates the need for transduction from its extracellular binding site to the intracellular region. This picture was obtained from PubMed]]

[[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane. This image depicts the spanning of the membrane made by NTSR1 and illustrates the need for transduction from its extracellular binding site to the intracellular region. This picture was obtained from PubMed.]]

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/4'>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.

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/4'>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 ===

Binding of NTS to the binding site is enriched by <scene name='72/721539/Binding_pocket_surface/4'>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. The protein is colored by charge: negative and positive. Two of NTS's arginine residues are colored blue. In addition, the C-terminus of NTS forms a <scene name='72/721539/Binding_site_charges/4'>salt bridge</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] with R328 of NTSR1. Three [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 <scene name='72/721539/B-hairpin_loop/1'>Β-hairpin loop</scene> at the proximal end of the receptor protein's N-terminus.<ref name="White"/>

Sandbox reserved 1169: Difference between revisions

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@@ Line 11: / Line 11: @@
 == Structure ==
 === Overall Structure ===
-[[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane. This image depicts the spanning of the membrane made by NTSR1 and illustrates the need for transduction from its extracellular binding site to the intracellular region. This picture was obtained from PubMed]]
+[[Image:Nuerotensin membrane.jpg |100 px|left|thumb|Figure 1: Neurotensin Incorporation in Membrane. This image depicts the spanning of the membrane made by NTSR1 and illustrates the need for transduction from its extracellular binding site to the intracellular region. This picture was obtained from PubMed.]]
-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/4'>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.
+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/4'>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 ===
 Binding of NTS to the binding site is enriched by <scene name='72/721539/Binding_pocket_surface/4'>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. The protein is colored by charge: <font color='#FF0000'>negative</font> and <font color='#0000CD'>positive</font>. Two of NTS's arginine residues are colored <font color='#0000CD'>blue</font>. In addition, the C-terminus of <font color='#32CD32'>NTS</font> forms a <scene name='72/721539/Binding_site_charges/4'>salt bridge</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] with R328 of <font color='#A9A9A9'>NTSR1</font>. Three  [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 <scene name='72/721539/B-hairpin_loop/1'>Β-hairpin loop</scene> at the proximal end of the receptor protein's N-terminus.<ref name="White"/>