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Figure 4.
Analysis of the concatenated HER3 and HER4 kinase domains in
the crystal lattices. (A) Pattern of kinase monomer interactions
observed in the crystal lattices of the kinase domains of HER3
and inactive HER4 (PDB ID code 3BBW). The C-terminal tail
exchanging dimers are propagated through the N-lobe dimer
interface. JM refers to portion of the juxtamembrane segment.
(B) Detailed view of the HER3 and HER4 N-lobe dimers.
Hydrophobic residues are shown in stick representation. (C)
Empirical estimates of binding free energy of HER3 and HER4
N-lobe homodimers using conformations obtained from all-atom
molecular dynamics simulations. (D) Comparison between the
C-terminal tail interaction with the C-lobe in the HER3 kinase
domain dimer and the HER4 kinase domain dimer (PDB ID code 3BBW)
and interaction of Mig6/segment 1 with the C-lobe of the EGFR
kinase domain (PDB ID code 2RFE).
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