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Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP
Author(s): Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK
Source: CELL    Volume: 89    Issue: 6    Pages: 951-961    Published: JUN 13 1997  
Times Cited: 312     References: 64     
Abstract: The X-ray structure of the eukaryotic translation initiation factor 4E (elF4E), bound to 7-methyl-GDP, has been determined at 2.2 Angstrom resolution. elF4E 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. The convex dorsal surface of the molecule displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with other translation initiation factors and regulatory proteins.
Document Type: Article
Language: English
Addresses:
1. ROCKEFELLER UNIV, MOL BIOPHYS LAB, NEW YORK, NY 10021 USA
2. ROCKEFELLER UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA
3. MCGILL UNIV, DEPT BIOCHEM, MONTREAL, PQ H3G 1Y6 CANADA
4. MCGILL UNIV, MCGILL CANC CTR, MONTREAL, PQ H3G 1Y6 CANADA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: XE357
ISSN: 0092-8674
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