Sandbox Reserved 1387
From Proteopedia
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== Disease == | == Disease == | ||
| - | Defects in GLUT3 can cause fetal death as well as neurodegeneration, which can lead to diseases like Alzheimer’s. | + | Defects in GLUT3 can cause fetal death as well as neurodegeneration, which can lead to diseases like Alzheimer’s. In the case of Alzheimer's Disease (AD), the defective GLUT3 does not provide neurons with optimal glucose concentrations. Autopsies of AD patients have shown higher sugar concentrations in the brain's extracellular tissue while also possessing abnormally low GLUT3 counts. |
In Type 2 Diabetes patients, there is a decrease in the amount of transcripts that encode for GLUT3. | In Type 2 Diabetes patients, there is a decrease in the amount of transcripts that encode for GLUT3. | ||
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Its <scene name='77/777707/Hydrophobic_binding_sites/2'>Hydrophobic Binding Sites</scene> are Leucine, Alanine, Phenylalanine, Isoleucine. Its <scene name='77/777707/Hydrophilic_binding_sites/1'>Hydrophilic Binding Sites</scene> are Serine, Glutamic Acid, Arginine, Threonine. The interactions between the hydrophobic and hydrophylic groups allow GLUT3 to bind to octylglucose neopentylglycol and cholesterol hemisuccinate. Both of these substrates have polar and non-polar regions; they are precursors to simpler sugars. | Its <scene name='77/777707/Hydrophobic_binding_sites/2'>Hydrophobic Binding Sites</scene> are Leucine, Alanine, Phenylalanine, Isoleucine. Its <scene name='77/777707/Hydrophilic_binding_sites/1'>Hydrophilic Binding Sites</scene> are Serine, Glutamic Acid, Arginine, Threonine. The interactions between the hydrophobic and hydrophylic groups allow GLUT3 to bind to octylglucose neopentylglycol and cholesterol hemisuccinate. Both of these substrates have polar and non-polar regions; they are precursors to simpler sugars. | ||
| - | The protein's <scene name='77/777707/Non_polar_scene/1'>Non Polar Regions</scene> are understandably located on the exterior surface, since the complex is embedded in the lipid membrane. | + | The protein's <scene name='77/777707/Non_polar_scene/1'>Non Polar Regions</scene> are understandably located on the exterior surface, since the complex is embedded in the lipid membrane. Conversely, GLUT3's <scene name='77/777707/Polar_regions/1'>Polar Regions</scene> are located on the inside of the complex to interact with the substrates and hold the structure of the protein together. |
| - | + | ||
| - | Conversely, GLUT3's <scene name='77/777707/Polar_regions/1'>Polar Regions</scene> are located on the inside of the complex to interact with the substrates. | + | |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 04:17, 1 March 2018
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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Homo sapien Glucose Transporter GLUT3 / SLC2A3
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References
- ↑ https://www.ebi.ac.uk/pdbe/entry/pdb/5c65
- ↑ Simpson IA, Dwyer D, Malide D, Moley KH, Travis A, Vannucci SJ. The facilitative glucose transporter GLUT3: 20 years of distinction. Am J Physiol Endocrinol Metab. 2008 Aug;295(2):E242-53. doi:, 10.1152/ajpendo.90388.2008. Epub 2008 Jun 24. PMID:18577699 doi:http://dx.doi.org/10.1152/ajpendo.90388.2008
- ↑ doi: https://dx.doi.org/10.2147/CHC.S60484
- ↑ https://www.ebi.ac.uk/pdbe/entry/pdb/5c65
