2v6c

From Proteopedia

---

Revision as of 10:20, 23 January 2008

proteopedia linkproteopedia link

spinqualitylabelsall models 2v6c, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 Aug 9;. PMID:17690690

Page seeded by OCA on Wed Jan 23 12:20:44 2008