Druggability analysis of membrane proteins by DoGSiteScorer
- Published
- Accepted
- Subject Areas
- Biochemistry, Bioinformatics, Biophysics, Computational Biology
- Keywords
- druggability, HIV, membrane protein, DoGSiteScorer, phospholamban, glycoprotein-41
- Copyright
- © 2017 Zhang et al.
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
- Cite this article
- 2017. Druggability analysis of membrane proteins by DoGSiteScorer. PeerJ Preprints 5:e2868v1 https://doi.org/10.7287/peerj.preprints.2868v1
Abstract
Membrane proteins are the most medicinally important yet to be fully exploited pharmaceutical targets. Here druggability analyses are conducted on three different membrane proteins, namely, the human P2Y12 receptor, glycoprotein-41 that mediates the HIV-1 virus entry and membrane fusion, and phospholamban that regulates the Ca2+ pump in cardiac muscle cells. DoGSiteScorer, a grid-based bioinfromatic technology, is able to identify the binding pockets of all three membrane proteins, and the results were in great agreements with the available crystal structure of P2Y12 receptor-ligand complex. This druggability analysis is especially helpful in cases where the crystal structures of membrane protein-ligand complexes are still difficult to obtain. Better understanding of the druggable pockets of membrane proteins also requires including the membrane environment.
Author Comment
This is a preprint submission to PeerJ Preprints.