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. 2017 Jul 5;7:4656. doi: 10.1038/s41598-017-04844-w

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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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Integrin structure and N-linked glycosylation. (A) Cartoon models of integrin in the bent conformation. The domains are color-coded as same as panels B–D. (B,C) The distribution of potential N-glycan sites in the integrin α subunits without (B) or with (C) the αI-domain. The 7 blades of β-propeller domain are labeled. (D) The distribution of potential N-glycan sites in the integrin β subunits. The numbers of predicted N-linked glycosylation sites are shown on the right for each integrin subunit.