2nlw
From Proteopedia
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Solution structure of the RRM domain of human eukaryotic initiation factor 3b
Overview
Mammalian eIF3 is a 700 kDa multiprotein complex essential for initiation, of protein synthesis in eukaryotic cells. It consists of 13 subunits, (eIF3a-m), among which eIF3b serves as a major scaffolding protein. Here, we report the solution structure of the N-terminal RNA Recognition Motif, of human eIF3b (eIF3b-RRM) determined by NMR spectroscopy. The structure, reveals a non-canonical RRM with a negatively charged surface in the, beta-sheet area contradictory with potential RNA binding activity., Instead, eIF3j, which is required for stable 40S ribosome binding of the, eIF3 complex, specifically binds to the rear alpha-helices of the, eIF3b-RRM, opposite to its beta-sheet surface. Moreover, we identify that, an N-terminal 69 amino acid peptide of eIF3j is sufficient for binding to, eIF3b-RRM and that this interaction is essential for eIF3b-RRM recruitment, to the 40S ribosomal subunit. Our results provide the first structure of, an important subdomain of a core eIF3 subunit, and detailed insights into, protein-protein interactions between two eIF3 subunits required for stable, eIF3 recruitment to the 40S ribosome.
About this Structure
2NLW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of eIF3b-RRM and its interaction with eIF3j: Structural insights into the recruitment of eIF3b to the 40S ribosomal subunit., Elantak L, Tzakos AG, Locker N, Lukavsky PJ, J Biol Chem. 2006 Dec 26;. PMID:17190833
Page seeded by OCA on Mon Nov 12 22:59:23 2007
