Fig. 2 | Nature Communications

Fig. 2

From: Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01

Fig. 2

Key features of the binding interface between 2E3-Fab and HLA-A*11:01. a Aspartic acid at position 90 (Asp90) is the predicted eplet for 2E3 and is highlighted on the structure of A*11:01 (PDB 2HN7). b The structure of 2E3-Fab complexed with HLA-A*11:01 monomer was solved by X-ray crystallography at 2.4 Å. Fab fragment of 2E3 consists of heavy chain (blue ribbon) and light chain shown (pink ribbon). It interacts with refolded HLA-A*11:01 which comprises of α chain shown in white, β2m shown in green and a peptide shown as mesh. c Magnified view of the interaction between 2E3-Fab and HLA-A*11:01 near the predicted eplet (Asp90). The Asn31 of 2E3 light chain variable region interacts with Asp90 of HLA α chain. d View of interaction interface between 2E3-Fab and HLA-A*11:01, when KIR2DS2 (PDB 4N8V), e TCR (PDB 5WKH), and f CD8 (PDB 1AKJ) are bound to the same HLA molecule. HLA human leukocyte antigens

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