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Figure 2.
Figure 2 Comparison of Eph receptor KD crystal structures. (A)
Superposition of active Eph KD structures with auto-inhibited
EphB2 structures (PDB ID 1JPA). KDs were aligned using C^  atoms
of the C-lobes (left panel) and C^ atoms
of the N-lobes (right panel). Spheres represent the ordered
boundaries of the KD activation segment. (B) Stereo view of
kinked KD helices  C.
The Eph receptor KDs (colored as in panel A) were superimposed
using C^ atoms
of helix C.
The kink stabilizing side chains of Ser677 and Ser680 in
auto-inhibited EphB2 JMS-KD are shown in dark blue. (C) View of
the inter-lobe cleft, highlighting the ordered regions of the KD
activation segments (colored as in panel A). (D) Superposition
of EphB2 JMS-KD with the active Eph KD structures, highlighting
the region surrounding Tyr750. Backbone traces are colored as in
panel A, with all side chains colored according to their
respective backbones. The backbone of a typical activation
segment conformation from the active insulin RTK (1IR3) is shown
in magenta.
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