Sandbox GGC16: Difference between revisions

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<scene name='87/874948/Earbindingresiduesbest/1'>Residues at Binding Domain</scene>
<scene name='87/874948/Earbindingresiduesbest/1'>Residues at Binding Domain</scene>
Ets binding domain is conserved across the Ets family of proteins which consist of about 35 proteins with similar functions.  
Ets binding domain is conserved across the Ets family of proteins which consist of about 35 proteins with similar functions.  
Binding domain is positively charged. Residues most closely interacting with DNA include Arginine and Lysine. These are highly conserved- the two Arginines on the central helix within the major groove of the DNA and two Lysines on the outer turns.  
Binding domain is positively charged. Residues most closely interacting with DNA include Arginine and Lysine. These are highly conserved- the two Arginines on the central helix within the major groove of the DNA and two Lysines on the outer turns.<ref>Kodandapani, R., Pio, F., Ni, CZ. et al. A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex. Nature 380, 456–460 (1996). https://doi.org/10.1038/380456a0</ref>


== Disease ==
== Disease ==

Revision as of 18:33, 24 April 2021

PU.1

Caption for this structure

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References