2IF1
HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES
Summary for 2IF1
| Entry DOI | 10.2210/pdb2if1/pdb |
| NMR Information | BMRB: 4255 |
| Descriptor | EIF1 (1 entity in total) |
| Functional Keywords | translation initiation factor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 14327.20 |
| Authors | Fletcher, C.M.,Hellen, C.U.T.,Pestova, T.V.,Wagner, G. (deposition date: 1998-08-04, release date: 1999-05-18, Last modification date: 2024-05-29) |
| Primary citation | Fletcher, C.M.,Pestova, T.V.,Hellen, C.U.,Wagner, G. Structure and interactions of the translation initiation factor eIF1. EMBO J., 18:2631-2637, 1999 Cited by PubMed Abstract: eIF1 is a universally conserved translation factor that is necessary for scanning and involved in initiation site selection. We have determined the solution structure of human eIF1 with an N-terminal His tag using NMR spectroscopy. Residues 29-113 of the native sequence form a tightly packed domain with two alpha-helices on one side of a five-stranded parallel and antiparallel beta-sheet. The fold is new but similar to that of several ribosomal proteins and RNA-binding domains. A likely binding site is indicated by yeast mutations and conserved residues located together on the surface. No interaction with recombinant eIF5 or the initiation site RNA GCCACAAUGGCA was detected by NMR, but GST pull-down experiments show that eIF1 binds specifically to the p110 subunit of eIF3. This interaction explains how eIF1 is recruited to the 40S ribosomal subunit. PubMed: 10228174DOI: 10.1093/emboj/18.9.2631 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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