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. 2018 Jan 18;9:283. doi: 10.1038/s41467-017-02252-2

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© The Author(s) 2018

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 Commonslicense, unless indicated otherwise in a credit line to the material. If material is not included in the article’sCreative 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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Fig. 3 — Crystal structure of scFv45 and molecular explanation for scFv45 specificity for PTP1B-OX. a Crystal structure of scFv45 highlighting acidic residues Asp89, Glu88, and Asp93 in the complementarity-determining region (CDR). For representative numbering of scFv45 residues, the first amino acid denotes the residue directly following the OmpA cleavage site. b Molecular modeling of the PTP1B-OX:scFv45 complex, with PTP1B-OX shown in gray, and the regional boundaries of the scFv45-binding interface determined by our structural proteomic approach shown in yellow. The inset shows H-bonding between residues of PTP1B-OX (K41, Y46, and R47) and the acidic residues in the CDR of scFv45. c Surface electrostatic potential of PTP1B-OX (left), scFv45 (middle), and scFv20 (right)