PMID:17986575</ref> .
DiseaseRelevanceEts1 promotes invasive behavior in endothelial cells, smooth muscle cells and epithelial cancer cells.
Structural highlightsEts1 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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3D Structures of Ets13D Structures of Ets1
Updated on 10-February-2016
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- Ets1
- 1md0 – mETS1 ETS domain - mouse
- 1r36 – mETS1 ETS and autoinhibitory domains - NMR
- 2jv3, 2kmd – mETS1 PNT domain - NMR
- 1gvj – hETS1 ETS and autoinhibitory domains - human
- Ets1 binary complexes
- 2nny – hETS1 residues 280-441 + DNA
- 3mfk – hETS1 residues 280-441 + stromelysin promoter DNA
- 3ri4 – hETS1 residues 280-441 + TCR α promoter DNA
- 2stt, 2stw – hETS1 ETS domain + DNA - NMR
- 1k79, 1k7a – mETS1 ETS domain + DNA containing GGAA - mouse
- Ets1 ternary complexes
- 1mdm – mETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA
- 1k78 – hETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA - NMR
- 4l0y, 4l0z, 4l18 – hETS1 residues 296-441 + TCR α promoter DNA + RunT-related transcription factor
- 4lg0 – hETS1 residues 280-441 + cadherin promoter DNA + forkhead box protein
ReferencesReferences
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