Fig. 3: Detailed interactions between EBV or KSHV gHgL and EphA2 LBD. | Nature Communications

Fig. 3: Detailed interactions between EBV or KSHV gHgL and EphA2 LBD.

From: Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses

Fig. 3: Detailed interactions between EBV or KSHV gHgL and EphA2 LBD.

a, b Contact residues of the binding interface in the KSHV gHgL protein (a) or the EBV gHgL protein (b). The LBD-binding residues in KSHV gH and gL are colored blue and cyan, respectively; those in EBV gH and gL are colored smudge and yellow, respectively. c, d Contact residues of the binding interface in the LBD proteins. KSHV gH- and gL-binding residues are colored in violet and magenta, respectively; overlap binding residues are colored in red (c). EBV gH- and gL-binding residues are colored deep olive and orange, respectively; overlaping binding residues are colored yellow-orange (d). e, f Detailed hydrogen bond interactions between KSHV gHgL and LBD (e), and between EBV gHgL and LBD (f). g Detailed residues in LBD that interact with KSHV gHgL and EBV gHgL are shown in different colors; the area of each circle represents the number of contacts between gHgL and LBD. The residues binding to both KSHV and EBV gHgL with hydrogen bonds are colored in red. The residues binding only to KSHV gHgL with hydrogen bonds are colored magenta. The residues binding only to EBV gHgL with hydrogen bonds are colored orange.

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