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The PY-NLS of 2H4M contains a hydrophobic rather than a basic N-terminal motif. Hydrophobic interactions at the N-terminal motif of the PY-NLS include:  
The PY-NLS of 2H4M contains a hydrophobic rather than a basic N-terminal motif. Hydrophobic interactions at the N-terminal motif of the PY-NLS include:  
<scene name='37/372725/Kapb2_hydrophobic_interactions/3'>Phe273, Gly274, Pro275 and Met276 of the NLS with Trp730 and Ile773 of KapB2</scene>. Interactions of the C-terminal RX2-5PY motif of the NLS include: <scene name='37/372725/Hydrophobic_interactions_cterm/1'>Arg284 of the NLS with Glu509 and Asp543 of KapB2</scene>; <scene name='37/372725/Hydrophobic_interactions_cterm/2'>Pro288 and Tyr289 of the NLS with Ala380, Ala381, Asp384, Leu419, Ile457, Trp460 and Arg464 of KapB2.</scene>
<scene name='37/372725/Kapb2_hydrophobic_interactions/4'>Phe273, Gly274, Pro275 and Met276 of the NLS with Trp730 and Ile773 of KapB2</scene>. Interactions of the C-terminal RX2-5PY motif of the NLS include: <scene name='37/372725/Hydrophobic_interactions_cterm/1'>Arg284 of the NLS with Glu509 and Asp543 of KapB2</scene>; <scene name='37/372725/Hydrophobic_interactions_cterm/2'>Pro288 and Tyr289 of the NLS with Ala380, Ala381, Asp384, Leu419, Ile457, Trp460 and Arg464 of KapB2.</scene>


Upon binding Kapβ2,the NLS gains structure, conforms to and makes contact with the internal surface of the KapB2 C-terminal arch.
Upon binding Kapβ2,the NLS gains structure, conforms to and makes contact with the internal surface of the KapB2 C-terminal arch.

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Wayne Decatur, Student, Marisa L. VanBrakle, Allison Granberry