Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein
| Autor: | Anne-Claude Gingras, Nahum Sonenberg, Gerhard Wagner, Fletcher Cm, Hiroshi Matsuo, Hubo Li, Abigail Manson McGuire |
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| Rok vydání: | 1997 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Detergents Molecular Sequence Data Biology Antiparallel (biochemistry) RNA Cap Analogs Biochemistry Guanosine Diphosphate chemistry.chemical_compound Protein structure Structural Biology Peptide Initiation Factors Yeasts Genetics Translation factor Amino Acid Sequence Binding site Eukaryotic Initiation Factors Protein secondary structure Micelles Binding Sites EIF4G Binding protein Tryptophan Cholic Acids Crystallography Eukaryotic Initiation Factor-4E chemistry Helix Carrier Proteins |
| Zdroj: | Nature structural biology. 4(9) |
| ISSN: | 1072-8368 |
| Popis: | eIF4E, the mRNA cap binding protein, is a master switch that controls eukaryotic translation. To be active, it must bind eIF4G and form the eIF4F complex, which also contains eIF4A. Translation is downregulated by association of eIF4E with 4E-BP, which occupies the eIF4G binding site. Signalling events acting on 4E-BP cause it to dissociate from eIF4E, and eIF4E is then free to bind eIF4G to form the active eIF4F complex. We have solved the structure of the yeast eIF4E/m7Gpp complex in a CHAPS micelle. We determined the position of the second nucleotide in a complex with m7GpppA, and identified the 4E-BP binding site. eIF4E has a curved eight-stranded antiparallel beta-sheet, decorated with three helices on the convex face and three smaller helices inserted in connecting loops. The m7G of the cap is intercalated into a stack of tryptophans in the concave face. The 4E-BP binding site is located in a region encompassing one edge of the beta-sheet, the adjacent helix a2 and several regions of non-regular secondary structure. It is adjacent to, but does not overlap the cap-binding site. |
| Databáze: | OpenAIRE |
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