Sandbox Reserved 324: Difference between revisions

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"/>.