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Resolution: standard / high Figure 9.
Structure of RACK1 bound to the 40S eukaryotic ribosomal subunit and interaction with
co-associated ribosomal proteins. (A) Surface rendition of T. thermophila (PDB: 2XZN) 40S subunit: rRNA (white); RACK1 coloured as in Figure 2A/B; ribosomal proteins
are shown in grey with the exception of those in direct contact with RACK1 -- rpS3e
(light brown), rpS16e (light blue), rpS17e (pale cyan). (B) As (A) but with 90° rotation
about the y-axis; position of mRNA exit tunnel is marked (dashed oval). (C) Detail
of ribosome-bound RACK1 structure, highlighting PKC-binding loci on blades 2 and 6;
RACK1 and rRNA are shown in ribbon format, interacting ribosomal proteins are surface-rendered.
(D) Detail of key contacts between RACK1 residues (italicised) and rpS17e residues
(non-italicised): D27 (rpS17e) forms a salt bridge with R47 (RACK1); F30 (rpS17e)
packs against aromatic RACK1 side chains (W, Y, W, W). R47 (RACK1) engages rRNA backbone
phosphates.
Adams et al. Cell Communication and Signaling 2011 9:22 doi:10.1186/1478-811X-9-22 |