Detail publikace

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

HADDAD, Y. REMEŠ, M. ADAM, V. HEGER, Z.

Originální název

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

Typ

článek v časopise ve Web of Science, Jimp

Jazyk

angličtina

Originální abstrakt

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.

Klíčová slova

Structure-Based Drug Design; epidermal growth factor receptor (EGFR); kinase domain; molecular docking

Autoři

HADDAD, Y.; REMEŠ, M.; ADAM, V.; HEGER, Z.

Vydáno

28. 2. 2021

ISSN

1359-6446

Periodikum

DRUG DISCOVERY TODAY

Ročník

26

Číslo

2

Stát

Spojené království Velké Británie a Severního Irska

Strany od

289

Strany do

295

Strany počet

7

URL

https://www.sciencedirect.com/science/article/pii/S1359644620304220

BibTex

@article{BUT170589,
  author="Yazan Abdulmajeed Eyadh {Haddad} and Marek {Remeš} and Vojtěch {Adam} and Zbyněk {Heger}",
  title="Toward structure-based drug design against the epidermal growth factor receptor (EGFR)",
  journal="DRUG DISCOVERY TODAY",
  year="2021",
  volume="26",
  number="2",
  pages="289--295",
  doi="10.1016/j.drudis.2020.10.007",
  issn="1359-6446",
  url="https://www.sciencedirect.com/science/article/pii/S1359644620304220"
}