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. Author manuscript; available in PMC: 2011 Jul 18.
Published in final edited form as: Mol Biosyst. 2011 Apr 20;7(6):2066–2080. doi: 10.1039/c0mb00345j

Table 1.

Hydrogen bonding analysis of the HER3 MD trajectory and comparison to the MD trajectories for the active and inactive conformations of EGFR, HER2 and HER4. The bonds are organized by sub-domain, and bonds that are conserved in EGFR, HER2, and HER4 but not in HER3 are highlighted in bold. HER3 lacks many of the conserved bonds present in the active EGFR, HER2 and HER4 systems

EGFR active HER2 active HER4 active EGFR inactive HER2 inactive HER4 inactive HER3 inactive
αC-helix A-loop bonds
E739,R841
E734,K851 E766,K883 E739,K856
D737,K836 D769,R868 D742,R841
E738,F832 E743,F837 – –
E738,K836 E743,R841
αC-helix C-loop bonds
E743,R817
αC-helix bonds
A763,S760
E766,R756
E738,K721 E770,K753 E743,K726
M742,L753 M774,L785 M747,L758
A743,L679 A748,Q684
A748,R757
C-loop C-loop bonds
H843,D845 H813,N815
R812,D813 R844,D845
D813,R817 D845,R849 D818,R822
D813,N818 N815,N820
A815,N818 A847,N850 A820,N823 A815,N818 A847,N850 A817,N820
A848,V851
A-loop C-loop bonds
G865,V842
G838,R817
L834,R812 L866,R844 L839,R817
L834,D813
K836,V810 R868,V842 R841,V815
D838,R814
E848,R812
K851,R812
A-loop bonds
D836,K726 D863,K753 D836,K726 D833,K723
D836,T835
L838,R808 L870,R840 L843,R813
D871,R840
A840,G672
D873,R897
D844,K853
K848,T873
K843,D932 K848,D937
E876,R898
E849,K871
Y845,Y867 Y850,F872
H846,R865
D880,R897 D853,R870 E848,R865 D880,R897 D853,R870