5J3V

Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail

5J3V の概要

• エントリーDOI: 10.2210/pdb5j3v/pdb
• 分子名称: Transportin-1,Transportin-1, Histone H3 (2 entities in total)
• 機能のキーワード: karyopherin, importin, transporting, histone, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 197109.84

構造登録者

Soniat, M.,Chook, Y.M. (登録日: 2016-03-31, 公開日: 2016-09-21, 最終更新日: 2023-09-27)

主引用文献

Soniat, M.,Chook, Y.M.
Karyopherin-beta 2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif.
Structure, 24:1802-1809, 2016

PubMed Abstract: Karyopherin-β2 or Transportin-1 binds proline-tyrosine nuclear localization signals (PY-NLSs) in its cargos. PY-NLSs are described by structural disorder, overall positive charge, and binding epitopes composed of an N-terminal hydrophobic or basic motif and a C-terminal R-XP-Y motif. The N-terminal tail of histone H3 binds Kapβ2 with high affinity but does not contain a recognizable PY-NLS. The crystal structure of the Kapβ2-H3 tail shows residues 11-27 of H3 binding to the PY-NLS site of Kapβ2. H3 residues TGGKAPRK bind the site for PY-NLS Epitope 1 (N-terminal hydrophobic/basic motif), which is most important for Kapβ2-binding. H3 residue Arg26 occupies the PY-NLS Epitope 2 position (usually arginine of R-XP-Y) but PY-NLS Epitope 3 (proline-tyrosine motif) is missing in the H3 tail. Histone H3 thus provides an example of a PY-NLS variant with no proline-tyrosine or homologous proline-hydrophobic motif. The H3 tail uses a very strong Epitope 1 to compensate for loss of the often-conserved proline-tyrosine epitope.

PubMed: 27618664
DOI: 10.1016/j.str.2016.07.018

実験手法

X-RAY DIFFRACTION (3.05 Å)