Sandbox Reserved 344: Difference between revisions

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 ===Regulatory Domain===
 The regulatory domain consists of 5 α-helixes and 5 β-sheets. Twofold symmetry is achieved on the
-<scene name='Sandbox_Reserved_344/Dimerization_surface/1'>TextToBeDisplayed</scene> α-4 helix, β-5 sheet and α-5 helix face. The regulatory domain may be phosphorylated at a conserved  aspartate by PhoQ, a histidine protein kinase. Phosphorylation of this aspartate stabilizes the homodimer.<ref name = "Bachh2007"/>
+<scene name='Sandbox_Reserved_344/Dimerization_surface/1'>α-4 helix, β-5 sheet and α-5 helix face</scene> . The regulatory domain may be phosphorylated at a conserved  aspartate by PhoQ, a histidine protein kinase. Phosphorylation of this aspartate stabilizes the homodimer.<ref name = "Bachh2007"/>
 The PhoP regulatory domain has intrinsic autophosphatase activity, allowing it to inactivate itself after a delay.<ref name = "Perron-S"> PMID:16339942</ref>