5J3V
Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail
Summary for 5J3V
| Entry DOI | 10.2210/pdb5j3v/pdb |
| Descriptor | Transportin-1,Transportin-1, Histone H3 (2 entities in total) |
| Functional Keywords | karyopherin, importin, transporting, histone, transport protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 197109.84 |
| Authors | Soniat, M.,Chook, Y.M. (deposition date: 2016-03-31, release date: 2016-09-21, Last modification date: 2023-09-27) |
| Primary citation | 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 Cited by 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: 27618664DOI: 10.1016/j.str.2016.07.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.05 Å) |
Structure validation
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