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Crystal structure of human nuclear pore complex component NUP43
Author(s) -
Xu Chao,
Li Zhihong,
He Hao,
Wernimont Amy,
Li Yanjun,
Loppnau Peter,
Min Jinrong
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.09.008
Subject(s) - nuclear pore , component (thermodynamics) , crystal structure , crystallography , chemistry , crystal (programming language) , materials science , physics , biochemistry , computer science , cytoplasm , programming language , thermodynamics
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.