2J76

Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B

Summary for 2J76

• Entry DOI: 10.2210/pdb2j76/pdb
• Related: 1WI8
• Descriptor: EUKARYOTIC TRANSLATION INITIATION FACTOR 4B (1 entity in total)
• Functional Keywords: protein biosynthesis, rna recognition motif, initiation factor, rna binding domain, translation, rrm, rbd, rnp, rna-binding, phosphorylation
• Biological source: HOMO SAPIENS
• Total number of polymer chains: 1
• Total formula weight: 11457.73

Authors

Fleming, K.,Ghuman, J.,Yuan, X.M.,Simpson, P.,Szendroi, A.,Matthews, S.,Curry, S. (deposition date: 2006-10-06, release date: 2008-10-28, Last modification date: 2024-05-15)

Primary citation

Fleming, K.,Ghuman, J.,Yuan, X.M.,Simpson, P.,Szendroi, A.,Matthews, S.,Curry, S.
Solution Structure and RNA Interactions of the RNA Recognition Motif from Eukaryotic Translation Initiation Factor 4B.
Biochemistry, 42:8966-, 2003

PubMed Abstract: Eukaryotic initiation factor 4B (eIF4B) is a multidomain protein with a range of activities that serves primarily to promote association of messenger RNA to the 40S ribosomal subunit during translation initiation. We report here the solution structure of the eIF4B RNA recognition motif (RRM) domain. It adopts a classical RRM fold, with a beta alpha beta beta alpha beta topology. The most striking difference with other RRM structures is in the disposition of loop 3, which connects the beta 2 and beta 3 strands and is implicated in RNA recognition. This loop folds down against the body of the RRM and exhibits restricted motion on a milli- to microsecond time scale. Although it contributes to a large basic patch on the RNA binding surface, it does not protrude out from the domain as observed in other RRM structures, possibly implying a different mode of RNA binding. On its own, the core RRM domain provides only a relative weak interaction with RNA targets and appears to require extensions at the N- and C-terminus for high-affinity binding.

PubMed: 12885229
DOI: 10.1021/BI034506G

Experimental method

SOLUTION NMR