Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain

Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain

Erlotinib and gefitinib, tyrosine kinase inhibitors used to block EGFR (epidermal growth factor receptor) signalling in cancer, are thought to bind only the active conformation of the EGFR-TKD (tyrosine kinase domain). Through parallel computational and crystallographic studies, we show in the prese...

Full description

Bibliographic Details
Main Authors: Park, Jin H., Liu, Yingting, Lemmon, Mark A., Radhakrishnan, Ravi
Format: Online
Language:English
Published: Portland Press Ltd. 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507260/
id pubmed-3507260
recordtype oai_dc
spelling pubmed-35072602012-11-27 Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain Park, Jin H. Liu, Yingting Lemmon, Mark A. Radhakrishnan, Ravi Accelerated Publication Erlotinib and gefitinib, tyrosine kinase inhibitors used to block EGFR (epidermal growth factor receptor) signalling in cancer, are thought to bind only the active conformation of the EGFR-TKD (tyrosine kinase domain). Through parallel computational and crystallographic studies, we show in the present study that erlotinib also binds the inactive EGFR-TKD conformation, which may have significant implications for its use in EGFR-mutated cancers. Portland Press Ltd. 2012-11-21 2012-12-15 /pmc/articles/PMC3507260/ /pubmed/23101586 http://dx.doi.org/10.1042/BJ20121513 Text en © 2012 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Park, Jin H.
Liu, Yingting
Lemmon, Mark A.
Radhakrishnan, Ravi
spellingShingle Park, Jin H.
Liu, Yingting
Lemmon, Mark A.
Radhakrishnan, Ravi
Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
author_facet Park, Jin H.
Liu, Yingting
Lemmon, Mark A.
Radhakrishnan, Ravi
author_sort Park, Jin H.
title Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
title_short Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
title_full Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
title_fullStr Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
title_full_unstemmed Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
title_sort erlotinib binds both inactive and active conformations of the egfr tyrosine kinase domain
description Erlotinib and gefitinib, tyrosine kinase inhibitors used to block EGFR (epidermal growth factor receptor) signalling in cancer, are thought to bind only the active conformation of the EGFR-TKD (tyrosine kinase domain). Through parallel computational and crystallographic studies, we show in the present study that erlotinib also binds the inactive EGFR-TKD conformation, which may have significant implications for its use in EGFR-mutated cancers.
publisher Portland Press Ltd.
publishDate 2012
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507260/
_version_ 1611935689698443264

Similar Items