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. 2017 Sep 14;7:11587. doi: 10.1038/s41598-017-11886-7

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Structure simulation and masking efficiency analysis of pro-anti-EGFR antibodies. (A) Computer molecular dynamic simulation of anti-EGFR Fab structure with hollow sphere (purple). The CDRs of light chain (light blue) and heavy chain (yellow) are additionally marked to distinguish them from the Fab structure (blue). The protein structures of LAP-Fab (B), C2b-Fab (C) and CBa-Fab (D) are shown with hollow spheres (purple). A smaller sphere volume indicates a greater masking efficiency of the inhibitory domain. The sphere volumes were calculated to measure the masking efficiency of the LAP domain (orange), C2b (red) and CBa (green) over the binding sites of Fab.