2if1
From Proteopedia
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'''HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES''' | '''HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES''' | ||
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[[Category: Pestova, T V.]] | [[Category: Pestova, T V.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:25:46 2008'' | |
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Revision as of 04:25, 4 May 2008
HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES
Overview
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.
About this Structure
2IF1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and interactions of the translation initiation factor eIF1., Fletcher CM, Pestova TV, Hellen CU, Wagner G, EMBO J. 1999 May 4;18(9):2631-7. PMID:10228174 Page seeded by OCA on Sun May 4 07:25:46 2008
