Fig. 4: Comparison of the LNK SH2 domain bound to JAK2 pY813 and EPOR pY454 phosphopeptides. | Nature Communications

Fig. 4: Comparison of the LNK SH2 domain bound to JAK2 pY813 and EPOR pY454 phosphopeptides.

From: Structural and functional analysis of target recognition by the lymphocyte adaptor protein LNK

Fig. 4

a Alignment of the backbone of the WT LNK SH2 domain from the JAK2 pY813 bound structure (red) and the EPOR pY454 bound structure (purple) with secondary structural features indicated. b The pY813 JAK2 (black) and EPOR pY454 (white) peptides bound to the SH2 domain show a high degree of similarity. c The +1 Leu of the EPOR pY454 peptide is positioned in a hydrophobic surface on the LNK SH2 domain (left). The +1 Glu of the JAK2 pY813 peptide is positioned over the same surface, however the carboxylate also forms a salt bridge interaction with Lys 384 of LNK (middle). The LNK SH2 BG loop of the EPOR pY454 bound structure is displaced by approximately 5 Å in comparison to the JAK2 pY813 bound structure (red) (right).

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