Sandbox Reserved 814
From Proteopedia
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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. | ||
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+ | 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. | |
Revision as of 21:42, 8 January 2014
RIBOSOMAL PROTEIN L14
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This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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