4KA3

Structure of MAP kinase in complex with a docking peptide

Summary for 4KA3

• Entry DOI: 10.2210/pdb4ka3/pdb
• Descriptor: Mitogen-activated protein kinase 14, TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (3 entities in total)
• Functional Keywords: kinase domain, phosphorylation, kim, transferase-protein binding complex, transferase/protein binding
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm: P47811
• Total number of polymer chains: 2
• Total formula weight: 44506.64

Authors

Xin, F.J.,Wu, J.W. (deposition date: 2013-04-22, release date: 2013-06-26, Last modification date: 2023-11-08)

Primary citation

Xin, F.J.,Wu, J.W.
Crystal structure of the p38 alpha MAP kinase in complex with a docking peptide from TAB1
Sci China Life Sci, 56:653-660, 2013

PubMed Abstract: The mitogen-activated protein kinase (MAPK) p38α is a key regulator in many cellular processes, whose activity is tightly regulated by upstream kinases, phosphatases and other regulators. Transforming growth factor-β activated kinase 1 (TAK1) is an upstream kinase in p38α signaling, and its full activation requires a specific activator, the TAK1-binding protein (TAB1). TAB1 was also shown to be an inducer of p38α's autophosphorylation and/or a substrate driving the feedback control of p38α signaling. Here we determined the complex structure of the unphosphorylated p38α and a docking peptide of TAB1, which shows that the TAB1 peptide binds to the classical MAPK docking groove and induces long-range conformational changes on p38α. Our structural and biochemical analyses suggest that TAB1 is a reasonable substrate of p38α, yet the interaction between the docking peptide and p38α may not be sufficient to trigger trans-autophosphorylation of p38α.

PubMed: 23722236
DOI: 10.1007/s11427-013-4494-0

Experimental method

X-RAY DIFFRACTION (2.707 Å)