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Revision as of 18:25, 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

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Function(s) and Biological Relevance
2 Broader Implications
3 Structural highlights and structure-function relationships
4 Energy Transformation

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 labeled in brown. (Fernandez-Justel, David, et al. pg. 14768).

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. (Fernandez-Justel, David, et al. pg. 14768).

Structural highlights and structure-function relationships

This view shows the of the protein. The protein hydrophobicity can determine how it interacts with other molecules or proteins.

This shows view. This view shows the molecules in purple.

This view shows the parts in yellow. The negative area shows the phosphate backbone as well.

This view shows the areas. (Fernandez-Justel, David, et al. pg. 14768-14771).

Energy Transformation

The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity. View. Dinucleoside polyphosphates modulate the catalytic activity of IMPDHs in vitro by efficiently competing with the adenine/guanine mono nucleotides for the allosteric sites. (Fernandez-Justel, David, et al. pg. 14768).

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

Fernandez-Justel, David, et al. "The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates." Journal of Biological Chemistry, vol. 294, no. 40, 2019, pp. 14768-14775., doi:10.1074/jbc.ac119.010055.

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1557"

@@ Line 20: / Line 20: @@
 == Energy Transformation ==
 The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity.
-<scene name='82/823081/Transparent/1'>Transparent</scene> View. Dinucleoside polyphosphates modulate the catalytic activity of IMPDHs in vitro by efficiently competing with the adenine/guanine mono nucleotides for the allosteric sites. <scene name='82/823081/Adenine_guanine_sites/1'>Adenine_Guanine Sites</scene>
+<scene name='82/823081/Transparent/1'>Transparent</scene> View. Dinucleoside polyphosphates modulate the catalytic activity of IMPDHs in vitro by efficiently competing with the adenine/guanine mono nucleotides for the allosteric sites. <scene name='82/823081/Adenine_guanine_sites/1'>Adenine_Guanine Sites</scene> (Fernandez-Justel, David, et al. pg. 14768).
 </StructureSection>
 == References ==
 <references/> Fernandez-Justel, David, et al. "The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates." Journal of Biological Chemistry, vol. 294, no. 40, 2019, pp. 14768-14775., doi:10.1074/jbc.ac119.010055.

Sandbox Reserved 1557

From Proteopedia

Revision as of 18:25, 30 November 2019

IMP dehydrogenase Structure and Function

Contents

Function(s) and Biological Relevance

Broader Implications

Structural highlights and structure-function relationships

Energy Transformation

References

Views

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