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TitleIdentification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM.
Journal, issue, pagesNat Struct Mol Biol, Vol. 11, Issue 10, Page 957-962, Year 2004
Publish dateAug 29, 2004
AuthorsJayati Sengupta / Jakob Nilsson / Richard Gursky / Christian M T Spahn / Poul Nissen / Joachim Frank /
PubMed AbstractRACK1 serves as a scaffold protein for a wide range of kinases and membrane-bound receptors. It is a WD-repeat family protein and is predicted to have a beta-propeller architecture with seven blades ...RACK1 serves as a scaffold protein for a wide range of kinases and membrane-bound receptors. It is a WD-repeat family protein and is predicted to have a beta-propeller architecture with seven blades like a Gbeta protein. Mass spectrometry studies have identified its association with the small subunit of eukaryotic ribosomes and, most recently, it has been shown to regulate initiation by recruiting protein kinase C to the 40S subunit. Here we present the results of a cryo-EM study of the 80S ribosome that positively locate RACK1 on the head region of the 40S subunit, in the immediate vicinity of the mRNA exit channel. One face of RACK1 exposes the WD-repeats as a platform for interactions with kinases and receptors. Using this platform, RACK1 can recruit other proteins to the ribosome.
External linksNat Struct Mol Biol / PubMed:15334071
MethodsEM (single particle)
Resolution11.7 Å
Structure data

PDB-1trj:
Homology Model of Yeast RACK1 Protein fitted into 11.7A cryo-EM map of Yeast 80S Ribosome
Method: ELECTRON MICROSCOPY / Resolution: 11.7 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsSIGNALING PROTEIN / RACK1 / Ribosome / homology model

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