Figure 3: Structure of JNK1 in complex with MKP7-CD. | Nature Communications

Figure 3: Structure of JNK1 in complex with MKP7-CD.

From: A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation

Figure 3

(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan. The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan). The JNK1 is shown in surface representation coloured according to electrostatic potential (positive, blue; negative, red). (e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1. MKP7-CD is shown in surface representation coloured according to electrostatic potential (positive, blue; negative, red). Blue dashed lines represent polar interactions. (f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.

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