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Fig. 1. (A) Schematic domain organization of the mature InlB and HGF proteins. For InlB: Cp, cap region; LRR, leucine-rich repeats; IR, inter-repeat region; B, B-repeats; GW, GW-repeats. For HGF, N, N-terminal domain; K, kringles; SP, serine protease homology region. The mature heterodimer is formed by proteolytic digestion at an Arg-Val site and linkage of the resulting {alpha} and ß chains by a disulfide bridge (S-S). (B) Crystal structure of the LRR domain of InlB [reproduced from (Marino et al., 1999)]. The domain consists of the N-terminal cap region (residues 36-76) and the LRR region (residues 77-242). {alpha} and 310 helices are in cyan, ß strands are in red and loops are in green. Putative calcium ions bound to the cap region are shown as blue spheres.