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. Author manuscript; available in PMC: 2019 Feb 6.
Published in final edited form as: Structure. 2018 Jan 18;26(2):270–281.e4. doi: 10.1016/j.str.2017.12.012

Figure 2. Crystal structure of the LET-23 kinase domain.

Figure 2

(A) The structure of the inactive C. elegans LET-23 kinase domain in complex with AMP-PNP compared to the structures of the inactive human EGFR V924R kinase in complex with AMP-PNP (PDB ID: 5CNO) and active human EGFR kinase in complex with an ATP analog (PDB ID: 2GS6). (B) Detailed view of structural elements in the N-lobe of the LET-23 kinase domain overlaid on the structure of the inactive human EGFR V924R kinase domain (PDB ID: 5CNO) highlighting features of the C helix interaction with the activation loop. (C) Comparison of C-tail binding modes in inactive human EGFR V924R kinase domains (PDB ID: 5CNO) (left panel), active human EGFR kinase domain (PDB ID: 2GS6), and inactive LET-23 kinase domain. (D) Detailed view of interactions between the C-tail and the hinge region in the crystal structures of LET-23 and inactive human EGFR V924R kinase domains (PDB ID: 5CNO). (E) The left panel shows two LET-23 kinases interacting via the C-terminal tail/C-lobe interface observed in the crystal lattice. The two right panels highlight interactions in the C-lobe interface in LET-23 (middle panel) and EGFR (right panel) with the C-tail in LET-23 or Mig6 in EGFR (PDB ID: 2RFE). See also Figure S1.