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Affinity grid-based cryo-EM of PKC binding to RACK1 on the ribosome
- Source :
- Journal of Structural Biology. 181:190-194
- Publication Year :
- 2013
- Publisher :
- Elsevier BV, 2013.
-
Abstract
- Affinity grids (AG) are specialized EM grids that bind macromolecular complexes containing tagged proteins to obtain maximum occupancy for structural analysis through single-particle EM. In this study, utilizing AG, we show that His-tagged activated PKC βII binds to the small ribosomal subunit (40S). We reconstructed a cryo-EM map which shows that PKC βII interacts with RACK1, a seven-bladed β-propeller protein present on the 40S and binds in two different regions close to blades 3 and 4 of RACK1. This study is a first step in understanding the molecular framework of PKC βII/RACK1 interaction and its role in translation.
- Subjects :
- Models, Molecular
Ribosome Subunits, Small, Eukaryotic
Protein Conformation
Cryoelectron Microscopy
Receptors, Cell Surface
Translation (biology)
Biology
Receptors for Activated C Kinase
Ribosome
Article
Neoplasm Proteins
Cell biology
GTP-binding protein regulators
Protein structure
GTP-Binding Proteins
Structural Biology
Ribosome Subunits
Protein Biosynthesis
Humans
Eukaryotic Small Ribosomal Subunit
Protein Kinase C
Protein kinase C
Subjects
Details
- ISSN :
- 10478477
- Volume :
- 181
- Database :
- OpenAIRE
- Journal :
- Journal of Structural Biology
- Accession number :
- edsair.doi.dedup.....856c79d623ff37e0b3205ddbdfcc335e