Sandbox reserved 1651: Difference between revisions

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For instance, <scene name='87/872232/Subunit_dhdds/1'>DHDDS</scene> missense mutations can provoke an autosomal recessive Retinitis pigmentosa (arRP). These mutations concern the S1 and S2 sites of the active site where pyrophosphate can bind and most of the mutations related to the disease impact directly the substrate binding, according to scientists. For one mutation, <scene name='87/872232/K42/3'>K42E</scene>, it is more complicated. Scientists remarked that this mutation can associate itself with the other mutation <scene name='87/872232/E234/1'>E234</scene> via a salt bridge, which provokes in the protein scale, hypothetically, an interaction with the adjacent active-site residues positively charged. Experiments revealed the stable salt bridge between K42E and E234 but also another stable salt bridge with the <scene name='87/872232/R38/1'>R38</scene> residue. Finally, experiments proved that aberrant polar networks are due to the K42E mutation, disturbing the active-site residues which can’t interact with the substrate and leading to a decrease of the catalytic activity [1].
For instance, <scene name='87/872232/Subunit_dhdds/1'>DHDDS</scene> missense mutations can provoke an autosomal recessive Retinitis pigmentosa (arRP). These mutations concern the S1 and S2 sites of the active site where pyrophosphate can bind and most of the mutations related to the disease impact directly the substrate binding, according to scientists. For one mutation, <scene name='87/872232/K42/3'>K42E</scene>, it is more complicated. Scientists remarked that this mutation can associate itself with the other mutation <scene name='87/872232/E234/1'>E234</scene> via a salt bridge, which provokes in the protein scale, hypothetically, an interaction with the adjacent active-site residues positively charged. Experiments revealed the stable salt bridge between K42E and E234 but also another stable salt bridge with the <scene name='87/872232/R38/1'>R38</scene> residue. Finally, experiments proved that aberrant polar networks are due to the K42E mutation, disturbing the active-site residues which can’t interact with the substrate and leading to a decrease of the catalytic activity [1].


== Structural highlights ==
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


</StructureSection>
</StructureSection>
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