Sandbox Reserved 814: Difference between revisions

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Protein-protein interactions are essential for the stability of ribosomes. The L14 subunits presents a perfect hydrophobic area on its structure too allow such an interaction with other ribosome’s subunits. This area is on the beta-barrel and is composed of <scene name='56/568012/Hydrophobarea/3'>four residues</scene> : Leu25, Val40, Val57 and Ile2. This area is very exposed and separated from the RNA binding site. Links to L4, L7/L12, L10, L11, L17 and L19 has been showed and are allowed by this hydrophobic structure.
Protein-protein interactions are essential for the stability of ribosomes. The L14 subunits presents a perfect hydrophobic area on its structure too allow such an interaction with other ribosome’s subunits. This area is on the beta-barrel and is composed of <scene name='56/568012/Hydrophobarea/3'>four residues</scene> : Leu25, Val40, Val57 and Ile2. This area is very exposed and separated from the RNA binding site. Links to L4, L7/L12, L10, L11, L17 and L19 has been showed and are allowed by this hydrophobic structure.
In the L14 subunit, there are also two binding sites for the fixation of the rRNA. These two sites could each bind to a specific RNA sequence and induce the folding of the 23S rRNA.


== Role of the L14 subunit ==
== Role of the L14 subunit ==


 
The ribosome orchestrates the synthesis of proteins in all cells.The rRNA three dimensional organization is a major element in the activity of the ribonucleoprotein complex. This three dimensional structure is organized by the ribosomal proteins.
 
Sequence alignment show that the structure of the L14 I highly conserved. It’s probably due to the fact that both mechanism and structure of the ribosome are common in all organisms.