Conformational studies of glucose transporter 1 (GLUT1) as an anticancer drug target
Molecules, ISSN: 1420-3049, Vol: 24, Issue: 11
2019
- 26Citations
- 124Usage
- 50Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations26
- Citation Indexes26
- CrossRef26
- 26
- Usage124
- Downloads110
- Abstract Views14
- Captures50
- Readers50
- 50
- Mentions1
- Blog Mentions1
- Blog1
Article Description
Glucose transporter 1 (GLUT1) is a facilitative glucose transporter overexpressed in various types of tumors; thus, it has been considered as an important target for cancer therapy. GLUT1 works through conformational switching from an outward-open (OOP) to an inward-open (IOP) conformation passing through an occluded conformation. It is critical to determine which conformation is preferred by bound ligands because the success of structure-based drug design depends on the appropriate starting conformation of the target protein. To find out the most favorable GLUT 1 conformation for ligand binding, we ran systemic molecular docking studies for different conformations of GLUT1 using known GLUT1 inhibitors. Our data revealed that the IOP is the preferred conformation and that residues Phe291, Phe379, Glu380, Trp388, and Trp412 may play critical roles in ligand binding to GLUT1. Our data suggests that conformational differences in these five amino acids in the different conformers of GLUT1 may be used to design ligands that inhibit GLUT1.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85067256621&origin=inward; http://dx.doi.org/10.3390/molecules24112159; http://www.ncbi.nlm.nih.gov/pubmed/31181707; https://www.mdpi.com/1420-3049/24/11/2159; https://digitalcommons.unmc.edu/cop_pharmsci_articles/23; https://digitalcommons.unmc.edu/cgi/viewcontent.cgi?article=1025&context=cop_pharmsci_articles; https://dx.doi.org/10.3390/molecules24112159
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