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Michael Soniat, Yuh Min Chook  Structure 

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Presentation on theme: "Michael Soniat, Yuh Min Chook  Structure "— Presentation transcript:

1 Karyopherin-β2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif 
Michael Soniat, Yuh Min Chook  Structure  Volume 24, Issue 10, Pages (October 2016) DOI: /j.str Copyright © Terms and Conditions

2 Figure 1 Sequence of the Histone H3 Tail and Structure of the Kapβ2-H3 Tail Complex (A) Domain organization of human histone H3. The segment of H3 (residues 1–47) used in co-crystallization with Kapβ2 is underlined, and the segment modeled in the crystal structure is colored cyan. (B) The 3.05 Å resolution crystal structure of Kapβ2 (pink) bound to histone H3 tail (cyan). (C) The Kapβ2-H3 tail interface with contacts ≤4.0 Å shown as dashed lines. (D) The mFo − DFc difference map (contoured at 2σ, gray mesh) at the H3 tail binding site of Kapβ2. The difference map, calculated prior to modeling of the H3 tail, is shown here with the H3 tail. Structure  , DOI: ( /j.str ) Copyright © Terms and Conditions

3 Figure 2 Comparison of the H3 Tail with hnRNP A1PY-NLS, hnRNP MPY-NLS, and FUSPY-NLS (A) Alignment of Histone H3 tail residues 11–27 with the PY-NLSs of hnRNP M, hnRNP A1, and FUS. The sequences are aligned based on superposition of the Kapβ2-H3 tail, Kapβ2-hnRNP MPY-NLS (PDB: 2OT8), Kapβ2-hnRNP A1PY-NLS (PDB: 2H4M), and Kapβ2-FUSPY-NLS (PDB: 4FDD) structures. Sequences in Epitope 1 are in yellow (hydrophobic motifs) or blue (basic motifs, sequences in Epitope 2 are red, and sequences in Epitope 3 are green. (B) Comparison of the H3 tail (cyan) with hnRNP MPY-NLS (yellow). Superposition of Kapβ2 residues 200–800 gives a Cα RMSD of 1.25 Å. PY-NLS Epitopes 1, 2, and 3 of hnRNP MPY-NLS are labeled. (C) Comparison of the H3 tail (cyan) with hnRNP A1PY-NLS (purple). Kapβ2s of the two complexes were superimposed (Cα RMSD 1.5 Å, superposition of Kapβ2 residues 200–800). (D) Comparison of the H3 tail (cyan) with FUSPY-NLS (orange). Superposition of Kapβ2 residues 200–800 gives a Cα RMSD of 1.74 Å. Structure  , DOI: ( /j.str ) Copyright © Terms and Conditions

4 Figure 3 Comparison of Kapβ2-PY-NLS Contacts
(A–L) Contacts (≤4 Å) between Kapβ2 (pink) and four different PY-NLSs (the H3 tail [cyan], hnRNP MPY-NLS [yellow], hnRNP A1PY-NLS [purple], and FUSPY-NLS [orange]) are shown as dashed lines. (A)–(D) show Kapβ2-NLS contacts in the Epitope 1 site, (E)–(H) show contacts in the Epitope 2 site, and (I)–(L) show contacts in the Epitope 3 site. Structure  , DOI: ( /j.str ) Copyright © Terms and Conditions


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