Crystal structure of human nuclear pore complex component NUP43.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Xu C,Li Z,He H,Wernimont A,Li Y,Loppnau P,Min J

doi

10.1016/j.febslet.2015.09.008

subject

Has Abstract

pub_date

2015-10-24 00:00:00

pages

3247-53

issue

21

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(15)00825-X

journal_volume

589

pub_type

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