Sandbox Reserved 1557
From Proteopedia
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== Function(s) and Biological Relevance == | == Function(s) and Biological Relevance == | ||
| - | IMP dehydrogenase is an enzyme that catalyzes the rate limiting de novo guanine nucleotide biosynthetic pathway. This protein comes from a fungus known as Ashbya gossypii. The pathway represents a therapeutic for managing several diseases, including microbial infections and cancer. . Dinucleoside polyphosphates play important physiological roles in the allosteric regulation of IMPDHs and may have important implications for the design of therapeutic strategies to inhibit IMPDHs. IMP dehydrogenase helps make it easier to make a purine, without it, it is very complicated. Here shows a view of the <scene name='82/823081/Purine/1'>Purines</scene> labeled in brown. | + | IMP dehydrogenase is an enzyme that catalyzes the rate limiting de novo guanine nucleotide biosynthetic pathway. This protein comes from a fungus known as Ashbya gossypii. The pathway represents a therapeutic for managing several diseases, including microbial infections and cancer. . Dinucleoside polyphosphates play important physiological roles in the allosteric regulation of IMPDHs and may have important implications for the design of therapeutic strategies to inhibit IMPDHs. IMP dehydrogenase helps make it easier to make a purine, without it, it is very complicated. Here shows a view of the <scene name='82/823081/Purine/1'>Purines</scene> labeled in brown. (Fernandez-Justel, David, et al. pg. 14768). |
== Broader Implications == | == Broader Implications == | ||
| - | Dinucleoside polyphosphates have been described to play a part in increasing variety of cellular processes like DNA replication and repair, cell division, nuerotransmission, apoptosis, analgesia, vasoconstriction, and platlet aggregation. As it is described to play a part in these cellular processes, there is also others not mentioned it is known to play a role in. Dinucleoside polyphosphates have been described to interact with several target protiens including adenylate kinase, purinergic receptors, heat shock protiens, and poly(A) polymerase among others. | + | Dinucleoside polyphosphates have been described to play a part in increasing variety of cellular processes like DNA replication and repair, cell division, nuerotransmission, apoptosis, analgesia, vasoconstriction, and platlet aggregation. As it is described to play a part in these cellular processes, there is also others not mentioned it is known to play a role in. Dinucleoside polyphosphates have been described to interact with several target protiens including adenylate kinase, purinergic receptors, heat shock protiens, and poly(A) polymerase among others. (Fernandez-Justel, David, et al. pg. 14768). |
== Structural highlights and structure-function relationships == | == Structural highlights and structure-function relationships == | ||
This view shows the <scene name='82/823081/Hydrophobicity/1'>Hyrdrophobicity</scene> of the protein. The protein hydrophobicity can determine how it interacts with other molecules or proteins. | This view shows the <scene name='82/823081/Hydrophobicity/1'>Hyrdrophobicity</scene> of the protein. The protein hydrophobicity can determine how it interacts with other molecules or proteins. | ||
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This view shows the <scene name='82/823081/Acidic_and_or_negative/1'>Acidic/Negative</scene> parts in yellow. The negative area shows the phosphate backbone as well. | This view shows the <scene name='82/823081/Acidic_and_or_negative/1'>Acidic/Negative</scene> parts in yellow. The negative area shows the phosphate backbone as well. | ||
| - | This view shows the <scene name='82/823081/Basic_positive/1'>Basic_Positive </scene> areas. | + | This view shows the <scene name='82/823081/Basic_positive/1'>Basic_Positive </scene> areas. (Fernandez-Justel, David, et al. pg. 14768-14771). |
== Energy Transformation == | == Energy Transformation == | ||
The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity. | The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity. | ||
Revision as of 18:24, 30 November 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. |
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IMP dehydrogenase Structure and Function
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
