Sandbox Reserved 324: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
{{Template:Sandbox_Reserved_BCMB307}} | {{Template:Sandbox_Reserved_BCMB307}} | ||
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
='''Human eIF2α (1q8k)'''= | ==='''Human eIF2α (1q8k)'''=== | ||
{{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}} | {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}} | ||
| Line 9: | Line 9: | ||
=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 eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two<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"/>. | ||
=Function= | =Function= | ||
