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. Author manuscript; available in PMC: 2022 Dec 1.
Published in final edited form as: Nature. 2021 Nov 10;600(7888):339–343. doi: 10.1038/s41586-021-04084-z

Extended Data Fig. 4 |. Comparison of the domain II dimerization interface between HER2/HER3/NRG1β complex domain with crystal structures of previously reported HER receptor homodimers.

Extended Data Fig. 4 |

a-e, The domain II interfaces of select HER receptor dimers are shown with the number of hydrogen bonds and the total buried surface area between domains I-III indicated below. Domain IV was excluded from this analysis because it is not resolved in all structures. Hydrogen bonds are shown as red dotted lines, highlighting more substantial interfaces for symmetric homodimers (EGFR/EGF (PDB ID 3NJP), HER4/NRG1β (PDB ID 3U7U) than asymmetric dimers (HER2/HER3/NRG1β, EGFR/EREG (PDB ID 5WB7)), with the exception of the mutant HER2-S310F/HER3/NRG1β heterocomplex in which the mutation stabilizes the domain II interface. All interface hydrogen bonds are formed within domain II, except for an additional hydrogen bond in EGFR with domain III which is not shown here and marked (*) in table.