Art:Opening a Gate to Human Health: Difference between revisions

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[[Image:PDBe.png|150 px|right]]

[[Image:Oct2017.png|400 px|right]]

'''Behind the Artwork and the Protein Structure'''

In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. It is one of these molecules which features in this artwork, created by Alice Clark from PDBe. It shows ivermectin bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism. The scientists suggest FXR as a potential mammalian drug target of ivermectin.

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'''How Ivermectin Works'''

In organisms affected by Ivermectin, it causes paralysis and ultimately death. It binds to glutamate-gated chloride channels - proteins in the membranes of nerve and muscle cells which let in chloride ions to pass the signal along. Because Ivermectin binds specifically to channels in invertebrates it leaves the channels in vertebrate cells, such as those in humans, unaffected. It specifically binds to the membrane spanning region (PDB entry [[~~3RI5~~]]), causing the channel to be stuck on ‘open’. This leads to increased permeability of chloride ions across the membrane and the inability of the nerves to pass on signals.

In organisms affected by Ivermectin, it causes paralysis and ultimately death. It binds to glutamate-gated chloride channels - proteins in the membranes of nerve and muscle cells which let in chloride ions to pass the signal along. Because Ivermectin binds specifically to channels in invertebrates it leaves the channels in vertebrate cells, such as those in humans, unaffected. It specifically binds to the membrane spanning region (PDB entry [[3ri5]]), causing the channel to be stuck on ‘open’. This leads to increased permeability of chloride ions across the membrane and the inability of the nerves to pass on signals.

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+[[Image:PDBe.png|150 px|right]]
 [[Image:Oct2017.png|400 px|right]]
+'''Behind the Artwork and the Protein Structure'''
 In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. It is one of these molecules which features in this artwork, created by Alice Clark from PDBe. It shows ivermectin bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism. The scientists suggest FXR as a potential mammalian drug target of ivermectin.
@@ Line 19: / Line 22: @@
 '''How Ivermectin Works'''
-In organisms affected by Ivermectin, it causes paralysis and ultimately death. It binds to glutamate-gated chloride channels - proteins in the membranes of nerve and muscle cells which let in chloride ions to pass the signal along. Because Ivermectin binds specifically to channels in invertebrates it leaves the channels in vertebrate cells, such as those in humans, unaffected. It specifically binds to the membrane spanning region (PDB entry [[3RI5]]), causing the channel to be stuck on ‘open’. This leads to increased permeability of chloride ions across the membrane and the inability of the nerves to pass on signals.
+In organisms affected by Ivermectin, it causes paralysis and ultimately death. It binds to glutamate-gated chloride channels - proteins in the membranes of nerve and muscle cells which let in chloride ions to pass the signal along. Because Ivermectin binds specifically to channels in invertebrates it leaves the channels in vertebrate cells, such as those in humans, unaffected. It specifically binds to the membrane spanning region (PDB entry [[3ri5]]), causing the channel to be stuck on ‘open’. This leads to increased permeability of chloride ions across the membrane and the inability of the nerves to pass on signals.