3FEY

Crystal structure of the CBC-importin alpha complex.

Summary for 3FEY

• Entry DOI: 10.2210/pdb3fey/pdb
• Related: 3FEX
• Descriptor: Nuclear cap-binding protein subunit 1, Nuclear cap-binding protein subunit 2, Importin subunit alpha-2, ... (4 entities in total)
• Functional Keywords: cap binding complex, importin alpha, nuclear transport, mrna transport, nucleus, phosphoprotein, rna-binding, host-virus interaction, translation, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q09161 P52298; Cytoplasm: P52292
• Total number of polymer chains: 3
• Total formula weight: 160767.96

Authors

Dias, S.M.G.,Ambrosio, A.L.B.,Cerione, R.A. (deposition date: 2008-12-01, release date: 2009-08-11, Last modification date: 2023-09-06)

Primary citation

Dias, S.M.,Wilson, K.F.,Rojas, K.S.,Ambrosio, A.L.,Cerione, R.A.
The molecular basis for the regulation of the cap-binding complex by the importins.
Nat.Struct.Mol.Biol., 16:930-937, 2009

PubMed Abstract: The binding of capped RNAs to the cap-binding complex (CBC) in the nucleus, and their dissociation from the CBC in the cytosol, represent essential steps in RNA processing. Here we show how the nucleocytoplasmic transport proteins importin-alpha and importin-beta have key roles in regulating these events. As a first step toward understanding the molecular basis for this regulation, we determined a 2.2-A resolution X-ray structure for a CBC-importin-alpha complex that provides a detailed picture for how importin-alpha binds to the CBP80 subunit of the CBC. Through a combination of biochemical studies, X-ray crystallographic information and small-angle scattering experiments, we then determined how importin-beta binds to the CBC through its CBP20 subunit. Together, these studies enable us to propose a model describing how importin-beta stimulates the dissociation of capped RNA from the CBC in the cytosol following its nuclear export.

PubMed: 19668212
DOI: 10.1038/nsmb.1649

Experimental method

X-RAY DIFFRACTION (2.2 Å)