Sandbox Reserved 327: Difference between revisions
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<scene name='Sandbox_Reserved_327/Human_eif1/1'>human eIF1</scene> | <scene name='Sandbox_Reserved_327/Human_eif1/1'>human eIF1</scene> | ||
since the structure is similar to human eIF1 (87%) with 63% matched DNA composition (identity) <ref name="flet"/> <ref name="eIF1"/>. However, yeast eIF1 has two different conformations with two clear sets of backbone resonances for 13 of the 20 residues that lead to 20 different possible solution structure of yeast eIF1 <ref name="eIF1"/>. | since the structure is similar to human eIF1 (87%) with 63% matched DNA composition (identity) <ref name="flet"/> <ref name="eIF1"/>. However, yeast eIF1 has two different conformations with two clear sets of backbone resonances for 13 of the 20 residues that lead to 20 different possible solution structure of yeast eIF1 <ref name="eIF1"/>. | ||
==eIF1-ribosome binding site== | |||
The eIF1 would bind to the small subunit (40S) of a ribosome, in its P-site region. This binding would affect the conformation of the 40S subunit and the position of mRNA and the start codon initiation LOMAKIN. Surprisingly, this binding site region is similar to the binding site of prokaryotic initiation factor IF3 to the ribosome, despite their unrelated structure (LOMAKIN). | |||
==eIF1-eIF5 binding sites== | |||
There are two | |||
<scene name='Sandbox_Reserved_327/Basic_eif1/3'>eIF1-eIF5 binding sites</scene> | |||
: at the NTT site of eIF1 and at a KH surface area, a specific region that rich in Lysine (K) and hydrophobic (H) residues <ref name="eIF1"/>. These bindings are different from the eIF1-ribosome binding site and are salt dependent, with high salt concentration would make the interaction weaker <ref name="eIF1"/>. | |||
The eIF1-NTT area is believed to play role in stimulating the MFC assembly by promoting the eIF5- eIF2β <ref name="eIF1"/>. The other binding site area (eIF1-KH) is believed to play role in the AUG start codon selection in translation initiation <ref name="eIF1"/>. | |||
=Function and Mechanism= | =Function and Mechanism= | ||
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= | =Mutations= | ||
==eIF1-eIF5== | ==eIF1-eIF5== | ||
at the eIF1-eIF5 binding site | at the eIF1-eIF5 binding site | ||