4YR8

Crystal structure of JNK in complex with a regulator protein

Summary for 4YR8

• Entry DOI: 10.2210/pdb4yr8/pdb
• Descriptor: Mitogen-activated protein kinase 8, Dual specificity protein phosphatase 16, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: kinase domain, catalytic domain, transferase-hydrolase complex, transferase/hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : P45983 Q9BY84
• Total number of polymer chains: 8
• Total formula weight: 247139.27

Authors

Liu, X.,Wang, J.,Wu, J.W.,Wang, Z.X. (deposition date: 2015-03-14, release date: 2016-03-16, Last modification date: 2023-11-08)

Primary citation

Liu, X.,Zhang, C.S.,Lu, C.,Lin, S.C.,Wu, J.W.,Wang, Z.X.
A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation.
Nat Commun, 7:10879-10879, 2016

PubMed Abstract: Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs). MAPK signalling efficiency and specificity is modulated by protein-protein interactions between individual MAPKs and the docking motifs in cognate binding partners. Two types of docking interactions have been identified: D-motif-mediated interaction and FXF-docking interaction. Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction. The (285)FNFL(288) segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.

PubMed: 26988444
DOI: 10.1038/ncomms10879

Experimental method

X-RAY DIFFRACTION (2.4 Å)