1LEW

CRYSTAL STRUCTURE OF MAP KINASE P38 COMPLEXED TO THE DOCKING SITE ON ITS NUCLEAR SUBSTRATE MEF2A

Summary for 1LEW

• Entry DOI: 10.2210/pdb1lew/pdb
• Related: 1LEZ
• Descriptor: Mitogen-activated protein kinase 14, Myocyte-specific enhancer factor 2A (3 entities in total)
• Functional Keywords: protein-peptide complex, transferase, map kinase, serine/threonine-protein kinase, p38, mef2a
• Biological source: Mus musculus (Mouse); More
• Cellular location: Cytoplasm : P47811; Nucleus : Q02078
• Total number of polymer chains: 2
• Total formula weight: 42717.83

Authors

Chang, C.-I.,Xu, B.-E.,Akella, R.,Cobb, M.H.,Goldsmith, E.J. (deposition date: 2002-04-10, release date: 2002-07-10, Last modification date: 2024-02-14)

Primary citation

Chang, C.I.,Xu, B.E.,Akella, R.,Cobb, M.H.,Goldsmith, E.J.
Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b.
Mol.Cell, 9:1241-1249, 2002

PubMed Abstract: The structures of the MAP kinase p38 in complex with docking site peptides containing a phi(A)-X-phi(B) motif, derived from substrate MEF2A and activating enzyme MKK3b, have been solved. The peptides bind to the same site in the C-terminal domain of the kinase, which is both outside the active site and distinct from the "CD" domain previously implicated in docking site interactions. Mutational analysis on the interaction of p38 with the docking sites supports the crystallographic models and has uncovered two novel residues on the docking groove that are critical for binding. The two peptides induce similar large conformational changes local to the peptide binding groove. The peptides also induce unexpected and different conformational changes in the active site, as well as structural disorder in the phosphorylation lip.

PubMed: 12086621
DOI: 10.1016/S1097-2765(02)00525-7

Experimental method

X-RAY DIFFRACTION (2.3 Å)