Sandbox 125: Difference between revisions

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Kapβ2 is a superhelix comprised of 20 HEAT repeats (the name HEAT derives from Huntington, Elongation factor 3 A subunit of protein phosphatase 2A and Tor1 kinase), each of which consists of two anti-parallel helices. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. HEAT repeats 9-13 and 14-18 form the binding site of Kapβ2 cargos while repeats 1-8 constitute the Ran GTPase binding site.3 Ran GTPase, a small 216-residue protein, is found more frequently in the nucleus and enables cargos to be released from Kapβ2.  
Kapβ2 is a superhelix comprised of 20 HEAT repeats (the name HEAT derives from Huntington, Elongation factor 3 A subunit of protein phosphatase 2A and Tor1 kinase), each of which consists of two anti-parallel helices. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. HEAT repeats 9-13 and 14-18 form the binding site of Kapβ2 cargos while repeats 1-8 constitute the Ran GTPase binding site.3 Ran GTPase, a small 216-residue protein, is found more frequently in the nucleus and enables cargos to be released from Kapβ2.  


<font size=3> '''Kapβ2 Binding and Conformational Change''' </font>
<font size=3> '''Kapβ2 Binding and Conformational Change''' </font>
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Recognition of the PY-NLS by Kapβ2 follows certain guidelines:
Recognition of the PY-NLS by Kapβ2 follows certain guidelines:
(i) PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
(i) PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
(ii) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(ii) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(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.