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. 2015 Mar 27;16:103. doi: 10.1186/s12859-015-0528-x

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© Moonrin et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Graphical representation of root mean square fluctuation (RMSF) and superimposition of EGFR kinase. (A) The RMSF profiles of EGFR kinase bound MIG-6_s1 (in red), the unbound of EGFR kinase and MIG-6_s1 (in green), and EGFR kinase in the dimeric structure (in purple) with EGFR kinase (PDB: 2GS6). Most flexible regions can be seen as peaks in rectangles. (B) the superimposition of EGFR kinase monomers from 1) the unbound EGFR kinase (purple) 2) the EGFR kinase in the binding of MIG-6_s1 complex (orange) and 3) the dimer complex (green). The superimposition revealed the different mobility of the activation loop (A-loop).