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. 2019 Oct 29;9:15481. doi: 10.1038/s41598-019-50722-y

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© The Author(s) 2019

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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Crystal structure of unbound VHH. (a) Comparison of unbound D3-L11 (blue) with that in complex with HEL (green). HEL is shown in light purple. Overlaid structures using the three CDR loops. Backbone with the side chains of residues showing influence in binding (affinity loss >10-fold). (b) Enlarged view of the VHH binding interface from panel (a). The unbound and bound antibodies are depicted in cyan and gray, respectively; side chains of residues are shown with the same color gradient as that in Fig. 3.