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Figure 4.
FIGURE 4. Interactions in the SEI·HA·DR1,
SEH·HA·DR1, and SPEC·MBP·DR2a
interfaces. A, interactions between the HLA-DR1  -chain
(blue) and SEI (yellow) in the SEI·HA·DR1 complex.
The DR1  -chain (green) does not
contact SEI. Residues of the DR1 -chain involved in
interactions with SEI are green. The interface zinc ion is drawn
as a red sphere. Hydrogen bonds are represented as dashed lines.
Oxygen and nitrogen atoms are colored red and blue,
respectively. B, interactions between the HA peptide (pink) and
SEI (yellow). Peptide residues P–1 Lys and P2 Val (purple)
contact the SAG. C, Zn^2+ coordination in the
SEI·HA·DR1 complex. The zinc ion is tetrahedrally
coordinated by SEI residues His^169, His^207, and Asp^209
(yellow) and by HLA-DR1 residue His^81 (green). D, interactions
between the HLA-DR1 -chain (blue) and SEH
(yellow) in the SEH·HA·DR1 complex. Residues
Asp-55 and Asn^57 of the
DR1 -chain (green) also
contact SEH. E, interactions between the HA peptide (pink) and
SEH (yellow). Peptide residues P–1 Lys and P3 Lys (purple)
contact the SAG. F, Zn^2+ coordination in the
SEH·HA·DR1 complex. The zinc ion is coordinated by
SEH residues His^206 and Asp^208 (yellow) and by DR1 residue
His^81 (green). G, interactions
between the HLA-DR2a -chain (blue) and SPEC
(yellow) in the SPEC·MBP·DR2a complex. The DR2a
-chain (green) does not
contact SPEC. H, interactions between the MBP peptide (pink) and
SPEC (yellow). Peptide residues P–3 Val, P–2 His, P–1 Phe,
P2 Lys, and P3 Asn (purple) contact the SAG. I, Zn^2+
coordination in the SPEC·MBP·DR2a complex. The
zinc ion is coordinated tetrahedrally by SPEC residues His^167,
His^201, and Asp^203 (yellow) and by HLA-DR2a residue His^81
(green).
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