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Ets1

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Ets1 contains an ETS domain (residues 332-415) which is a helix-turn-helix DNA-binding domain which recognizes the sequence GGAA/T. The ETS domain is flanked by autoinhibitory domains. At the N-terminal, Ets1 contains a pointed domain (PNT) (residues 54-135) and a MAP kinase phosphorylation domain. PNT domain is related to SAM domains and contains 4 α-helices.
Ets1 contains an ETS domain (residues 332-415) which is a helix-turn-helix DNA-binding domain which recognizes the sequence GGAA/T. The ETS domain is flanked by autoinhibitory domains. At the N-terminal, Ets1 contains a pointed domain (PNT) (residues 54-135) and a MAP kinase phosphorylation domain. PNT domain is related to SAM domains and contains 4 α-helices.
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<scene name='59/595751/Cv/3'>Ets1 ETS domain with paired box protein Pax5 and MB-1 promoter DNA</scene> (PDB code [[1mdm]]).<ref>PMID:12221090</ref>
</StructureSection>
</StructureSection>

Revision as of 15:12, 10 February 2016

Structure of mouse Ets1 ETS domain (green) complex with paired box protein Pax5 (magenta) and MB-1 promoter DNA (PDB code 1mdm).

Drag the structure with the mouse to rotate

3D Structures of Ets1

Updated on 10-February-2016

References

  1. Garvie CW, Pufall MA, Graves BJ, Wolberger C. Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships. J Biol Chem. 2002 Nov 22;277(47):45529-36. Epub 2002 Sep 6. PMID:12221090 doi:10.1074/jbc.M206327200

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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