[HTML][HTML] Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity
EphA and EphB receptors preferentially bind ephrin-A and ephrin-B ligands, respectively,
but EphA4 is exceptional for its ability to bind all ephrins. Here, we report the crystal structure
of the EphA4 ligand-binding domain in complex with ephrin-B2, which represents the first
structure of an EphA-ephrin-B interclass complex. A loose fit of the ephrin-B2 GH loop in the
EphA4 ligand-binding channel is consistent with a relatively weak binding affinity. Additional
surface contacts also exist between EphA4 residues Gln 12 and Glu 14 and ephrin-B2 …
but EphA4 is exceptional for its ability to bind all ephrins. Here, we report the crystal structure
of the EphA4 ligand-binding domain in complex with ephrin-B2, which represents the first
structure of an EphA-ephrin-B interclass complex. A loose fit of the ephrin-B2 GH loop in the
EphA4 ligand-binding channel is consistent with a relatively weak binding affinity. Additional
surface contacts also exist between EphA4 residues Gln 12 and Glu 14 and ephrin-B2 …