5UMZ

Structure of TNRC6A NLS in complex with importin-alpha

Summary for 5UMZ

• Entry DOI: 10.2210/pdb5umz/pdb
• Descriptor: Importin subunit alpha-1, TNRC6A, GLYCEROL, ... (4 entities in total)
• Functional Keywords: mrna decay, mirna arm repeat, nuclear transport, protein transport
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 3
• Total formula weight: 58495.22

Authors

Chaston, J.,Stewart, A.G.,Christie, M. (deposition date: 2017-01-30, release date: 2017-12-27, Last modification date: 2023-10-04)

Primary citation

Chaston, J.J.,Stewart, A.G.,Christie, M.
Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha.
PLoS ONE, 12:e0183587-e0183587, 2017

PubMed Abstract: The GW182/TNRC6 family of proteins are central scaffolds that link microRNA-associated Argonaute proteins to the cytoplasmic decay machinery for targeted mRNA degradation processes. Although nuclear roles for the GW182/TNRC6 proteins are unknown, recent reports have demonstrated nucleocytoplasmic shuttling activity that utilises the importin-α and importin-β transport receptors for nuclear translocation. Here we describe the structure of mouse importin-α in complex with the TNRC6A nuclear localisation signal peptide. We further show that the interactions observed between TNRC6A and importin-α are conserved between mouse and human complexes. Our results highlight the ability of monopartite cNLS sequences to maximise contacts at the importin-α major binding site, as well as regions outside the main binding cavities.

PubMed: 28837617
DOI: 10.1371/journal.pone.0183587

Experimental method

X-RAY DIFFRACTION (1.9 Å)