Sandbox Reserved 1563: Difference between revisions

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<scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein.  Blue represents N-terminus.  Red represents C-terminus.
<scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein.  Blue represents N-terminus.  Red represents C-terminus.


<scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.
<scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.


<scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>.  In the space filled view we can see a better representation of how much space the protein would actually take up.  In the image the white is the protein as a whole and the red dots represent hydrogen bonds.
<scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>.  In the space filled view we can see a better representation of how much space the protein would actually take up.  In the image the white is the protein as a whole and the red dots represent hydrogen bonds.


<scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>.
<scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>.  For this image purple represent polar molecules and grey represents hydrophobic molecules.


<scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>.  In this view the black structures are the ACT molecules.  These are the ligands of the IMPDH protein.
<scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>.  In this view the black structures are the ACT molecules.  These are the ligands of the IMPDH protein.
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== '''Energy Transformation''' ==
== '''Energy Transformation''' ==


 
There are three binding sites within the bateman domain that regulate catalytic activity.  These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases.  Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain.  This requires the bateman domain to make IMPDH more sensitive to inhibition.  Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.
 
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>
== References ==
== References ==
1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.
1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.
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