X-ray studies of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP.

J. Marcotrigiano, A. C. Gingras, N. Sonenberg, S. K. Burley

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19 Scopus citations


The X-ray structure of the eukaryotic translation initiation factor 4E (eIF4E), bound to 7-methyl-GDP, has been determined at 2.2A resolution. eIF4E recognizes 5' 7-methyl-G(5')ppp(5')N mRNA caps during the rate-limiting initiation step of translation. The protein resembles a cupped hand, and consists of a curved, 8-stranded antiparallel beta-sheet, backed by three long alpha-helices. 7-methyl-GDP binds in a narrow cap-binding slot on the molecule's concave surface, where 7-methyl-guanine recognition is mediated by base sandwiching between two conserved tryptophans, plus formation of three hydrogen bonds and a van der Waals contact between its N7-methyl group and a third conserved tryptophan. Additional protein-ligand interactions include salt bridges and hydrogen bonds, plus water-mediated hydrogen bonds. The observed mode of 5' m-RNA cap recognition is almost certainly conserved among all known eIF4Es.

Original languageEnglish (US)
Pages (from-to)8-11
Number of pages4
JournalNucleic acids symposium series
Issue number36
StatePublished - 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Medicine


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