- Abstract:
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The epidermal growth factor receptor (EGFR) is a dimeric membrane protein which regulates key aspects of cellular function. Activation of the EGFR is linked to changes in the conformation of the transmembrane (TM) domain, brought about by changes in interactions of the TM helices of the membrane lipid bilayer. Using an advanced computational approach that combines coarse-grained molecular dynamics and well-tempered metadynamics, we characterize the large-scale motions of the TM helices, simul...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher version
- Files:
-
-
(pdf, 7.2mb)
-
- Publisher copy:
- 10.1021/jacs.6b05602
-
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- Funding agency for:
- Sansom, MSP
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Journal of the American Chemical Society Journal website
- Volume:
- 138
- Issue:
- 33
- Pages:
- 10611–10622
- Publication date:
- 2016-07-26
- DOI:
- EISSN:
-
1520-5126
- ISSN:
-
0002-7863
- Local pid:
- info:fedora/pubs:635434
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2016
- Notes:
- © 2016 American Chemical Society. This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Journal article
Conformational changes in the epidermal growth factor receptor: role of the transmembrane domain investigated by Coarse-Grained metadynamics free energy calculations
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+ Biotechnology and Biological Sciences Research Council
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