Crystal structure of human nuclear pore complex component NUP43

FEBS Lett. 2015 Oct 24;589(21):3247-53. doi: 10.1016/j.febslet.2015.09.008. Epub 2015 Sep 29.

Abstract

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.

Keywords: Nup107 subcomplex; Nup43; Nup85; Seh1L; WD40 repeat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray / methods*
  • Humans
  • Minor Histocompatibility Antigens
  • Models, Molecular
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / metabolism*
  • Protein Structure, Quaternary
  • Protein Structure, Secondary

Substances

  • Minor Histocompatibility Antigens
  • NUP133 protein, human
  • NUP43 protein, human
  • NUP85 protein, human
  • Nuclear Pore Complex Proteins