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Figure 1.
Figure 1: The EPEC/host-cell adhesion interface. The model is
based on our structural data of the complex of the C-terminal
fragment of intimin (domains D1, D2 and D3) and the
extracellular Tir IBD. Intimin is shown in green with domains
labelled and boundary residues numbered. The Ig-like domains D0,
D1 and D2 are shown as rectangles, and the lectin-like domain
D3, which binds to the Tir IBD, as an oval. Tir is shown as a
dimer (in pink and dark blue) in the host-cell membrane, and is
also labelled and numbered as described for intimin. The Tir IBD
is the extracellular component of Tir flanked by the two
predicted transmembrane (TM) domains. We observe a dimeric Tir
IBD, with the two helices in each monomer forming a four-helix
bundle that is stabilized by multiple hydrophobic and
hydrogen-bonded interactions. The N-terminal domain of Tir
anchors host cytoskeletal components (such as actin) that are
needed to form the characteristic A/E lesion on the host-cell
surface upon bacterial adhesion.
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