Figure 3.
FIGURE 3. SL9 peptides bound to HLA-A2. a, simulated (F[o]
– F[c]) omit map of SL9 peptide bound to HLA-A2. Electron
density within 5 Å of the peptide is contoured at the 2
level. Polypeptide
backbones of the [1] (gold) and [2](blue)
chains of HLA-A2 are indicated by ribbon diagram. b, CPK model
of the SL9 peptide built into the molecular surface of HLA-A2
rendered with convexity increasingly green and concavity
increasingly gray. c, the SL9-A3-HLA-A2 complex presented as in
b. Loss of the aromatic ring upon substitution of alanine for
tyrosine in P3 (position marked by arrows) leads to a cavity on
the MHC surface. Concomitantly, there is a complete loss of
detectable interaction between SL9-A3-HLA-A2 and D3.
level. Polypeptide
backbones of the 
[1] (gold) and 
[2](blue)
chains of HLA-A2 are indicated by ribbon diagram. b, CPK model
of the SL9 peptide built into the molecular surface of HLA-A2
rendered with convexity increasingly green and concavity
increasingly gray. c, the SL9-A3-HLA-A2 complex presented as in
b. Loss of the aromatic ring upon substitution of alanine for
tyrosine in P3 (position marked by arrows) leads to a cavity on
the MHC surface. Concomitantly, there is a complete loss of
detectable interaction between SL9-A3-HLA-A2 and D3.