Sandbox 130: Difference between revisions
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The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>. | The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>. | ||
'''How does Kapβ2 identify its cargo?''' | |||
The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. | The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. | ||
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(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus. | (iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus. | ||
The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and | The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: | ||
<scene name='37/372730/Backbone_arg92_94_96_/1'>Arg92, Arg94, Arg96</scene> of the NLS with Glu588 and Glu496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2. | |||
Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch. | Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch. | ||