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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/2'>Phe273, Gly274, Pro275 and Met276 of the NLS with Trp730 and Ile773 of KapB2</scene>. Interactions of the C-terminal R-X2-5-P-Y motif of the NLS include: Arg284 of the NLS with Glu509 and Asp543 of Kapβ2;  Pro288 and Tyr289 of the NLS with Ala380, Ala381, Asp384, Leu419, Ile457, Trp460 and Arg464 of Kapβ2.
<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 R-X2-5-P-Y motif of the NLS include: Arg284 of the NLS with Glu509 and Asp543 of Kapβ2;  Pro288 and Tyr289 of the NLS with Ala380, Ala381, Asp384, Leu419, Ile457, Trp460 and Arg464 of Kapβ2.


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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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