Sandbox 125: Difference between revisions

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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

Revision as of 01:03, 10 September 2013 view source Marisa L. VanBrakle (talk \| contribs) 146 edits No edit summary ← Older edit		Revision as of 23:43, 10 December 2013 view source Marisa L. VanBrakle (talk \| contribs) 146 edits No edit summary Newer edit →
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	<font size=3> '''Structure of Kapβ2''' </font>		<font size=3> '''Structure of Kapβ2''' </font>

	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 <scene name='37/372725/Kapb2_with_nls_heat_repeat1/1'>two anti-parallel helices</scene> (shown in red). The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. <font color='plum'><b> HEAT repeats </b></font> <scene name='37/372725/Kapb2_hr_9-13/2'>9-13</scene> and <scene name='37/372725/Kapb2_hr_14-18/1'>14-18</scene> 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 <scene name='37/372725/Kapb2_with_nls_heat_repeat1/1'>two anti-parallel helices</scene> (shown in red). The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative. <font color='plum'><b> HEAT repeats </b></font> <scene name='37/372725/Kapb2_hr_9-13/2'>9-13</scene> and <scene name='37/372725/Kapb2_hr_14-18/1'>14-18</scene> form the binding site of Kapβ2 cargos while repeats 1-8 constitute the Ran GTPase binding site. Ran GTPase, a small 216-residue protein, is found more frequently in the nucleus and enables cargos to be released from Kapβ2.