Sandbox GGC16
From Proteopedia
(Difference between revisions)
| Line 13: | Line 13: | ||
<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
| |||||||||||
References
- ↑ UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. (2021, April 7). Transcription factor PU.1. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. https://www.uniprot.org/uniprot/P17947.
- ↑ 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
