1N3K

Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)

Summary for 1N3K

• Entry DOI: 10.2210/pdb1n3k/pdb
• Descriptor: Astrocytic phosphoprotein PEA-15 (1 entity in total)
• Functional Keywords: death effector domain, six helix bundle, apoptosis
• Biological source: Cricetulus griseus (Chinese hamster)
• Cellular location: Cytoplasm: Q9Z297
• Total number of polymer chains: 1
• Total formula weight: 15061.08

Authors

Hill, J.M.,Vaidyanathan, H.,Ramos, J.W.,Ginsberg, M.H.,Werner, M.H. (deposition date: 2002-10-28, release date: 2003-01-14, Last modification date: 2024-05-22)

Primary citation

Hill, J.M.,Vaidyanathan, H.,Ramos, J.W.,Ginsberg, M.H.,Werner, M.H.
Recognition of ERK MAP Kinase by PEA-15 Reveals a Common Docking Site Within the Death Domain and Death Effector Domain
Embo J., 21:6494-6504, 2002

PubMed Abstract: PEA-15 is a multifunctional protein that modulates signaling pathways which control cell proliferation and cell death. In particular, PEA-15 regulates the actions of the ERK MAP kinase cascade by binding to ERK and altering its subcellular localization. The three-dimensional structure of PEA-15 has been determined using NMR spectroscopy and its interaction with ERK defined by characterization of mutants that modulate ERK function. PEA-15 is composed of an N-terminal death effector domain (DED) and a C-terminal tail of irregular structure. NMR 'footprinting' and mutagenesis identified elements of both the DED and tail that are required for ERK binding. Comparison of the DED-binding surface for ERK2 with the death domain (DD)-binding surface of Drosophila Tube revealed an unexpected similarity between the interaction modes of the DD and DED motifs in these proteins. Despite a lack of functional or sequence similarity between PEA-15 and Tube, these proteins utilize a common surface of the structurally similar DD and DED to recognize functionally diverse targets.

PubMed: 12456656
DOI: 10.1093/emboj/cdf641

Experimental method

SOLUTION NMR