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The locations of the HBGA binding interfaces are labeled by dashed circles.
In fact, different replacements of amino acids in the binding interfaces of both GI and GII NoVs are often seen, which serve as examples of some amino acids are replaceable in functional HBGA binding interfaces.
Human noroviruses (huNoVs) recognize histo-blood group antigens (HBGAs) as attachment factors, in which genogroup (G) I and GII huNoVs use distinct binding interfaces.
Additionally, multiple co-crystal structures of human IgG1 Fc with the low affinity FcγRs have allowed high resolution mapping of the binding interfaces.
Interaction networks between the terminal saccharides of HBGAs and the amino acids forming the binding interfaces have been thoroughly described [reviewed in (Tan and Jiang, 2014, 2011, 2010)].
Our data emphasize the complexity of NoV-HBGA interactions and highlight the role of human HBGAs in the evolution of HBGA binding interfaces of NoVs.
The two types of binding interfaces differ also in their binding modes to HBGAs.
Similarly, we generated and visualized electrostatic images of the TR binding interfaces (Vα and Vβ domains).
In addition, the binding interfaces in PPIs are generally highly conformationally flexible.
We analyzed the protein-nucleotide binding interfaces in these crystal structures using the PISA server [25].
These ligand binding sites correlate with known protein-protein binding interfaces required for oligomerization.
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