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1n3k
From Proteopedia
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'''Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)''' | '''Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)''' | ||
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[[Category: Vaidyanathan, H.]] | [[Category: Vaidyanathan, H.]] | ||
[[Category: Werner, M H.]] | [[Category: Werner, M H.]] | ||
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Revision as of 23:02, 2 May 2008
Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)
Overview
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.
About this Structure
1N3K is a Single protein structure of sequence from Cricetulus griseus. Full crystallographic information is available from OCA.
Reference
Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain., Hill JM, Vaidyanathan H, Ramos JW, Ginsberg MH, Werner MH, EMBO J. 2002 Dec 2;21(23):6494-504. PMID:12456656 Page seeded by OCA on Sat May 3 02:02:45 2008
