This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Reserved 1565
From Proteopedia
(Difference between revisions)
| Line 13: | Line 13: | ||
== Structural Highlights and Structure-Function Relationships == | == Structural Highlights and Structure-Function Relationships == | ||
| + | |||
| + | <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</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>. | ||
| + | |||
| + | <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene> | ||
| + | |||
| + | <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view | ||
| + | </scene>. | ||
| + | |||
| + | <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. | ||
| + | |||
| + | <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. | ||
| + | |||
| + | <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. | ||
| + | |||
| + | <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. | ||
== Energy Transformation == | == Energy Transformation == | ||
| + | |||
| + | |||
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. | 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. | ||
Revision as of 03:46, 1 December 2019
| This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575. |
To get started:
More help: Help:Editing |
Inosine-5'-monophosphate dehydrogenase
| |||||||||||
References
- ↑ Fernandez-Justel D, Pelaez R, Revuelta JL, Buey RM. The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates. J Biol Chem. 2019 Aug 15. pii: AC119.010055. doi: 10.1074/jbc.AC119.010055. PMID:31416831 doi:http://dx.doi.org/10.1074/jbc.AC119.010055
- ↑ Fernandez-Justel D, Pelaez R, Revuelta JL, Buey RM. The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates. J Biol Chem. 2019 Aug 15. pii: AC119.010055. doi: 10.1074/jbc.AC119.010055. PMID:31416831 doi:http://dx.doi.org/10.1074/jbc.AC119.010055
- ↑ Fernandez-Justel D, Pelaez R, Revuelta JL, Buey RM. The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates. J Biol Chem. 2019 Aug 15. pii: AC119.010055. doi: 10.1074/jbc.AC119.010055. PMID:31416831 doi:http://dx.doi.org/10.1074/jbc.AC119.010055
- ↑ Hedstrom L, Liechti G, Goldberg JB, Gollapalli DR. The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors. Curr Med Chem. 2011;18(13):1909-18. doi: 10.2174/092986711795590129. PMID:21517780 doi:http://dx.doi.org/10.2174/092986711795590129
- ↑ Bairagya HR, Mukhopadhyay BP. An insight to the dynamics of conserved water-mediated salt bridge interaction and interdomain recognition in hIMPDH isoforms. J Biomol Struct Dyn. 2012 Aug 28. PMID:22928911 doi:10.1080/07391102.2012.712458
