Sandbox Reserved 324: Difference between revisions
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The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA<sup>meti</sup> and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α <ref name="1q8k">PMID:15341733</ref>. | The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA<sup>meti</sup> and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α <ref name="1q8k">PMID:15341733</ref>. | ||
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=Structure= | =Structure= | ||
The human eIF2 structure was determined by NMR spectroscopy<ref name="1q8k"/>. The human eIF2 structure is a small structure made of two domains<ref name="1q8k"/>. These two domains have a unique characteristic in that they are mobile relative to the other domain<ref name="1q8k"/>. The N terminal domain (NTD) of the structure was discovered in previous years<ref name="nonato"> doi 10.1074/jbc.M111804200 </ref>. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold <ref name="nonato"/>. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain<ref name="nonato"/>. The second domain of the N terminus is a helical domain and it follows directly after the OB domain<ref name="nonato"/>. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain<ref name="nonato"/>. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove<ref name="nonato"/>. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two<ref name="1q8k"/>. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα<ref name="1q8k"/>. | The human eIF2 structure was determined by NMR spectroscopy<ref name="1q8k"/>. The human eIF2 structure is a small structure made of two domains<ref name="1q8k"/>. These two domains have a unique characteristic in that they are mobile relative to the other domain<ref name="1q8k"/>. The N terminal domain (NTD) of the structure was discovered in previous years<ref name="nonato"> doi 10.1074/jbc.M111804200 </ref>. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold <ref name="nonato"/>. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain<ref name="nonato"/>. The second domain of the N terminus is a helical domain and it follows directly after the OB domain<ref name="nonato"/>. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain<ref name="nonato"/>. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove<ref name="nonato"/>. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two<ref name="1q8k"/>. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα<ref name="1q8k"/>. | ||
