Sandbox 125: Difference between revisions
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(iii) General sequence for the PY-NLS is either a hydrophobic basic motif or a R-X2-5-P-Y motif at the C-terminus. | (iii) General sequence for the PY-NLS is either a hydrophobic basic motif or a R-X2-5-P-Y motif at the C-terminus. | ||
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: Phe273, Gly274, Pro275 and Met276 of the NLS with Trp730 and Ile773 of Kapβ2. 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. | 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/1'>Phe273, Gly274, Pro275 and Met276 of the NLS with Trp730 and Ile773 of Kapβ2</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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