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Figure 4.
Figure 4. Detailed View of the Interactions between InlA′
and hEC1(A) All residue side chains involved in direct
interactions or as ligands to bridging ions/water are indicated
in ball-and-stick representation. Residues mutated in this study
are underlined. For InlA′ β strands (1–15 and a of Ig-like
domain) and adjacent coils are shown in violet. hEC1 is
represented by a continuous coil, β strands are indicated by
dark-green shading (labels a–g, connecting loops are indicated
by two letters to indicate flanking β strands). Cyan-, yellow-
and orange-colored spheres represent water, Ca^2+, and Cl^−,
respectively.(B) View of the hydrophobic pocket in InlA′,
which accommodates Pro16 of hEC1. In addition, the neighboring
residues Phe17 (side chain omitted) and Pro18 are involved in
specific interactions with InlA′. Hydrogen bonds are indicated
by green dotted lines. In murine, E-cadherin Pro16 is replaced
by glutamate (yellow model).(C) The octahedrally coordinated
Ca^2+ bridging InlA′and hEC1. The refined 2F[O]-F[C] map
contoured at 1σ is shown as a translucent surface.
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