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. 2011 May 9;208(5):1041–1053. doi: 10.1084/jem.20100508

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© 2011 Ryan et al.

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Figure 1. — HLA-DR2 glycosylation sites and mechanism. (A) HLA-DR2 (DRA; DRB1*1501), shown with myelin basic protein peptide (green; space-filling), contains three N-glycosylation sites. The N78 position is highly conserved across species and is located at one end of the canonical peptide-binding groove, which is comprised of α-helices (blue) and a β-sheet foundation (red). Coordinates are from Gauthier et al., 1998. (B) Simplified N-glycosylation pathway in mammalian cells, highlighting the sites of CS (glucosidase inhibitor) and KF (mannosidase inhibitor) action and the representative structures expected. The asterisk highlights a complex N-glycan example from public data via the Consortium for Functional Glycomics. Specifically, this structure was found expressed by murine RAW macrophages, has a mass of 5035.3 Daltons, and is available in the dataset for A. Merrill request #1689 (http://www.functionalglycomics.org/glycomics/publicdata/glycoprofiling-new.jsp).