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. Author manuscript; available in PMC: 2014 Jan 8.
Published in final edited form as: Semin Immunopathol. 2012 Mar 30;34(3):10.1007/s00281-012-0309-9. doi: 10.1007/s00281-012-0309-9

Fig. 6.

Fig. 6

Structural model of Sp1 glycoantigen bound to human HLA-DR2 in the presence or absence of complex N-glycans. Images were created using previously defined crystal structures of HLA-DR2 [122] with modeled N-glycan structures (GLYCAM web tool [123]). The upper and lower images are showing different views of Sp1 (coordinates provided by Julia Wang [89]) associated with HLA-DR2 in the presence of attached triantennary complex N-glycans (left) or hybrid N-glycans (right). Alpha helices of the antigen binding groove are shaded blue and the rest of the molecule in green. The alpha chain N-glycan acceptor sites N78 and N118 are shown in orange as space-filled residues with the attached N-glycan structures shown in yellow and gray, respectively. The predicted association of a glycoantigen (Sp1 from S. pneumoniae; blue) is shown