【摘 要】
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Eukaryotic translation initiation factor eIF2B,the guanine nucleotide exchange factor(GEF)for eIF2,catalyzes composed of five subunits,α,β,γ,δ and ε,within
【机 构】
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National Laboratory of Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,Beijing
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Eukaryotic translation initiation factor eIF2B,the guanine nucleotide exchange factor(GEF)for eIF2,catalyzes composed of five subunits,α,β,γ,δ and ε,within which the ε,subunit is responsible for catalyzing the guanine exchange reaction.Here we present the crystal structure of the C-terminal domain of human eIF2Bε(eIF2Bε-CTD)at 2.0-A resolution.The structure resembles a HEAT motif and three charge-rich areas on its surface can be identified.When compared to yeast eIF2Bε-CTD,one area involves highly conserved AA boxes while the other two are only partially conserved,in addition,the previously reported mutations in human eIF2Bε-CTD,which are related to the loss of the GEF activity and human VWM disease,have been discussed.Based on the structure,most of such mutations tend to destabilize the HEAT motif.
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