Crystal structure of human nuclear pore complex component NUP43.
Nuclear pore complexes (NPC) form nuclear pores that cross the nuclear envelope and allow molecules to transport between the nucleus and the cytoplasm. We solved the crystal structure of human Nup43 (hNUP43), an important component in the Nup107 subcomplex of NPC. hNup43 adopts a seven-bladed β-propeller fold. We confirmed by ... ITC that neither human Nup37 (hNup37) nor human Nup133 (hNup133) interacts with hNup43. We demonstrated by analytical gel filtration that the human Nup85-Seh1L binary complex recruits hNup43 to form a ternary complex. Based on amino acid sequence analysis, we predicted the hNup85-hSeh1L binding surface of hNup43.
Mesh Terms:
Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Nuclear Pore Complex Proteins, Protein Structure, Quaternary, Protein Structure, Secondary
Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Nuclear Pore Complex Proteins, Protein Structure, Quaternary, Protein Structure, Secondary
FEBS Lett.
Date: Oct. 24, 2015
PubMed ID: 26391640
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