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. 2021 Jun 3;11:11663. doi: 10.1038/s41598-021-91165-8

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Purification and structure of anfibatide with GPIbα. (A) MALDI-TOF mass spectrometry showed a mass to charge ratio (m/z) of 29,799.7. Three-dimensional models of (B) structure of anfibatide (purple) integrated with GPIb (orange) and (C) VWF-A1 domain (green) and GPIbα complex from PDB entry 1SQ0⁴⁵ (https://www.rcsb.org/structure/1SQ0). (D) α-Thrombin (blue) and GPIbα complex from PDB entry 1OOK⁴⁴ (https://www.rcsb.org/structure/1OOK). Red arrows point to the sulfotyrosine region of GPIbα, the α-thrombin binding site. Protein-complex figures generated using Schrodinger PyMol 2 software (https://pymol.org/2/).