1n3k

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(New page: 200px<br /><applet load="1n3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n3k" /> '''Solution structure of phosphoprotein enriche...)
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'''Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)'''<br />
'''Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1N3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N3K OCA].
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1N3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3K OCA].
==Reference==
==Reference==
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[[Category: Cricetulus griseus]]
[[Category: Cricetulus griseus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ginsberg, M.H.]]
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[[Category: Ginsberg, M H.]]
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[[Category: Hill, J.M.]]
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[[Category: Hill, J M.]]
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[[Category: Ramos, J.W.]]
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[[Category: Ramos, J W.]]
[[Category: Vaidyanathan, H.]]
[[Category: Vaidyanathan, H.]]
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[[Category: Werner, M.H.]]
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[[Category: Werner, M H.]]
[[Category: death effector domain]]
[[Category: death effector domain]]
[[Category: six helix bundle]]
[[Category: six helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:56:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:53 2008''

Revision as of 12:01, 21 February 2008


1n3k

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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

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