2v6c

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(New page: 200px<br /><applet load="2v6c" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v6c, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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==Overview==
==Overview==
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The ErbB3-binding protein 1 (Ebp1) is an important regulator of, transcription, affecting eukaryotic cell growth, proliferation, differentiation and survival. Ebp1 can also affect translation and, cooperates with the polypyrimidine tract-binding protein (PTB) to, stimulate the activity of the internal ribosome entry site (IRES) of, foot-and-mouth disease virus (FMDV). We report here the crystal structure, of murine Ebp1 (p48 isoform), providing the first glimpse of the, architecture of this versatile regulator. The structure reveals a core, domain that is homologous to methionine aminopeptidases, coupled to a, C-terminal extension that contains important motifs for binding proteins, and RNA. It sheds new light on the conformational differences between the, p42 and p48 isoforms of Ebp1, the disposition of the key, protein-interacting motif ((354)LKALL(358)) and the RNA-binding activity, of Ebp1. We show that the primary RNA-binding site is formed by a Lys-rich, motif in the C terminus and mediates the interaction with the FMDV IRES., We also demonstrate a specific functional requirement for Ebp1 in FMDV, IRES-directed translation that is independent of a direct interaction with, PTB.
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The ErbB3-binding protein 1 (Ebp1) is an important regulator of transcription, affecting eukaryotic cell growth, proliferation, differentiation and survival. Ebp1 can also affect translation and cooperates with the polypyrimidine tract-binding protein (PTB) to stimulate the activity of the internal ribosome entry site (IRES) of foot-and-mouth disease virus (FMDV). We report here the crystal structure of murine Ebp1 (p48 isoform), providing the first glimpse of the architecture of this versatile regulator. The structure reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal extension that contains important motifs for binding proteins and RNA. It sheds new light on the conformational differences between the p42 and p48 isoforms of Ebp1, the disposition of the key protein-interacting motif ((354)LKALL(358)) and the RNA-binding activity of Ebp1. We show that the primary RNA-binding site is formed by a Lys-rich motif in the C terminus and mediates the interaction with the FMDV IRES. We also demonstrate a specific functional requirement for Ebp1 in FMDV IRES-directed translation that is independent of a direct interaction with PTB.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Structural insights into the transcriptional and translational roles of Ebp1., Monie TP, Perrin AJ, Birtley JR, Sweeney TR, Karakasiliotis I, Chaudhry Y, Roberts LO, Matthews S, Goodfellow IG, Curry S, EMBO J. 2007 Aug 9;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17690690 17690690]
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Structural insights into the transcriptional and translational roles of Ebp1., Monie TP, Perrin AJ, Birtley JR, Sweeney TR, Karakasiliotis I, Chaudhry Y, Roberts LO, Matthews S, Goodfellow IG, Curry S, EMBO J. 2007 Sep 5;26(17):3936-44. Epub 2007 Aug 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17690690 17690690]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Birtley, J.R.]]
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[[Category: Birtley, J R.]]
[[Category: Curry, S.]]
[[Category: Curry, S.]]
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[[Category: Monie, T.P.]]
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[[Category: Monie, T P.]]
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[[Category: Perrin, A.J.]]
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[[Category: Perrin, A J.]]
[[Category: acetylation]]
[[Category: acetylation]]
[[Category: cobalt]]
[[Category: cobalt]]
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[[Category: translational regulator]]
[[Category: translational regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:20:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:28 2008''

Revision as of 16:53, 21 February 2008

Image:2v6c.gif

2v6c, resolution 2.50Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF ERBB3 BINDING PROTEIN 1 (EBP1)

Overview

The ErbB3-binding protein 1 (Ebp1) is an important regulator of transcription, affecting eukaryotic cell growth, proliferation, differentiation and survival. Ebp1 can also affect translation and cooperates with the polypyrimidine tract-binding protein (PTB) to stimulate the activity of the internal ribosome entry site (IRES) of foot-and-mouth disease virus (FMDV). We report here the crystal structure of murine Ebp1 (p48 isoform), providing the first glimpse of the architecture of this versatile regulator. The structure reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal extension that contains important motifs for binding proteins and RNA. It sheds new light on the conformational differences between the p42 and p48 isoforms of Ebp1, the disposition of the key protein-interacting motif ((354)LKALL(358)) and the RNA-binding activity of Ebp1. We show that the primary RNA-binding site is formed by a Lys-rich motif in the C terminus and mediates the interaction with the FMDV IRES. We also demonstrate a specific functional requirement for Ebp1 in FMDV IRES-directed translation that is independent of a direct interaction with PTB.

About this Structure

2V6C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural insights into the transcriptional and translational roles of Ebp1., Monie TP, Perrin AJ, Birtley JR, Sweeney TR, Karakasiliotis I, Chaudhry Y, Roberts LO, Matthews S, Goodfellow IG, Curry S, EMBO J. 2007 Sep 5;26(17):3936-44. Epub 2007 Aug 9. PMID:17690690

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