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. 2019 Dec 2;10:5481. doi: 10.1038/s41467-019-13248-5

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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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Fig. 3 — Residues important in βI domain allostery. a–f The mobile portion of the βI domain is shown in a unliganded αVβ8, chain D; b liganded αVβ8, chain B; c liganded αVβ6 (4UM9, chain B); d liganded αIIbβ3 in state 1 (3ZDY, chain D); e liganded αIIbβ3 in state 7 (3ZDZ, chain B); and f liganded αIIbβ3 in state 8 (2VDR, chain B). Structure representation is as in Fig. 2, except that sidechain carbons are in silver and mainchain carbons are in green. Vertical dashed lines mark the position of the β-MIDAS motif D8 Cα atom in αIIbβ3 state 1 (d). g Sequences of all human integrin βI domains in regions that are important in ligand binding, shape shifting, or appear to have unusual residues in β8. Residues with sidechain or mainchain coordination to the MIDAS or ADMIDAS in typical integrins are asterisked in blue and orange, respectively. β-MIDAS residue positions and β8-subunit residue numbers are shown at the bottom.