Toward structure-based drug design against the epidermal growth factor receptor (EGFR)

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F21%3A43918477" target="_blank" >RIV/62156489:43210/21:43918477 - isvavai.cz</a>
Alternative codes found
RIV/00216305:26620/21:PU140216
Result on the web
<a href="https://doi.org/10.1016/j.drudis.2020.10.007" target="_blank" >https://doi.org/10.1016/j.drudis.2020.10.007</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.drudis.2020.10.007" target="_blank" >10.1016/j.drudis.2020.10.007</a>

Result language
angličtina
Original language name
Toward structure-based drug design against the epidermal growth factor receptor (EGFR)
Original language description
Most of the available crystal structures of epidermal growth factor receptor (EGFR) kinase domain, bound to drug inhibitors, originated from ligand-based drug design studies. Here, we used variations in 110 crystal structures to assemble eight distinct families highlighting the C-helix orientation in the N-lobe of the EGFR kinase domain. The families shared similar mutational profiles and similarity in the ligand R-groups (chemical composition, geometry, and charge) facing the C-helix, mutation sites, and DFG domain. For structure-based drug design, we recommend a systematic decision-making process for choice of template, guided by appropriate pairwise fitting and clustering before the molecular docking step. Alternatively, the binding site shape/volume can be used to filter and select the compound libraries. The article delineates structural features crucial for EGFR structure-based drug design and provides a rationale for the use of EGFR structure families for drug discovery applications.
Czech name
—
Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA18-10251S" target="_blank" >GA18-10251S: Comprehensive insight into mechanisms of action and metabolism of tyrosine kinase inhibitors and a study of ways increasing their antitumor efficiency</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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