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Sandbox Reserved 814

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== Bidding sites ==
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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.
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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.
== Role of the L14 subunit ==
== Role of the L14 subunit ==

Revision as of 21:41, 8 January 2014

RIBOSOMAL PROTEIN L14

Structure L14 ribosomal protein(PDB entry 1whi)

Drag the structure with the mouse to rotate
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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