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Fig. 3 | BMC Structural Biology

Fig. 3

From: The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins

Fig. 3

The putative conformational changes of DJNK upon peptide binding. a Global superposition of the DJNK bound to AMP-PNP with the JNK3-pepJIP1 complex. The regions of major structural changes upon peptide binding including the glycine-rich loop, the activation loop, the N-terminal MAPK insert (β1L0-β2L0 hairpin), αL16, αC, and αD are highlighted in green for JNK3-pJIP1 and cyan for DJNK, respectively, whereas the homologous regions are in grey color. b Close-up view of conformational changes in the ATP-binding and catalytic sites. Amino acid residues crucial for the ATP binding and catalytic activity of DJNK and JNK3-pepJIP1 are shown in cyan and green, respectively. The bound DJNK-AMP-PNP is shown in a magenta stick model. Two Mg2+ ions are shown as orange balls. Hydrogen bonds are indicated as dashed lines. c Sequence alignment of the docking sites of the scaffolding proteins JIP1 and APLIP1. The conserved residues are highlighted in red. d Close-up view of superposition of DJNK and JNK3-pepJIP1 in the peptide-binding sites. Amino acid residues crucial for the scaffold protein binding of DJNK and JNK3-pepJIP1 are labeled as in panel b, whereas the residues of pepJIP1 are presented in yellow sticks and labeled in black

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