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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 21:06, 15 August 2013 view source Marisa L. VanBrakle (talk \| contribs) 146 edits No edit summary ← Older edit		Revision as of 21:06, 15 August 2013 view source Marisa L. VanBrakle (talk \| contribs) 146 edits No edit summary Newer edit →
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	<font size=10> '''Structure of Kapβ2''' </font>		<font size=5> '''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 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.