|
|
| Line 31: |
Line 31: |
| **[[6da1]], [[6dat]] – mETS1 + SSR peptide <br /> | | **[[6da1]], [[6dat]] – mETS1 + SSR peptide <br /> |
|
| |
|
| *Ets1 ternary complexes | | *Ets1 higher complexes |
|
| |
|
| **[[1k78]] – hETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA - NMR<br /> | | **[[1k78]] – hETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA - NMR<br /> |
| Line 37: |
Line 37: |
| **[[4lg0]] – hETS1 residues 280-441 + cadherin promoter DNA + forkhead box protein<br /> | | **[[4lg0]] – hETS1 residues 280-441 + cadherin promoter DNA + forkhead box protein<br /> |
| **[[1mdm]] – mETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA <br /> | | **[[1mdm]] – mETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA <br /> |
| | **[[3wu1]] – hETS1 276-441 (mutant) + RUNX1 + DNA <br /> |
| | **[[3wts]], [[3wtt]], [[3wtu]], [[3wtv]], [[3wtw]], [[3wtx]], [[3wty]] – hETS1 276-441 (mutant) + RUNX1 + CBF beta + DNA <br /> |
|
| |
|
| }} | | }} |
Latest revision as of 11:29, 23 February 2023
| Function
Ets1 (E26 Transformation-Specific) or p54 is a proto-oncogene translation factor. Ets1 contributes to the regulation of cellular differentiation[1] .
Relevance
Ets1 promotes invasive behavior in endothelial cells, smooth muscle cells and epithelial cancer cells.
Structural highlights
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 ETS domain with paired box protein Pax5 and MB-1 promoter DNA (PDB code 1mdm).[2]
- ↑ Dwyer J, Li H, Xu D, Liu JP. Transcriptional regulation of telomerase activity: roles of the the Ets transcription factor family. Ann N Y Acad Sci. 2007 Oct;1114:36-47. PMID:17986575 doi:https://dx.doi.org/10.1196/annals.1396.022
- ↑ 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
|
3D Structures of Ets1
Updated on 23-February-2023
{"openlevels":0}
- Ets1
- 1mdm – hETS1 ETS and autoinhibitory domains - human
- 1md0 – mETS1 ETS domain - mouse
- 1r36 – mETS1 ETS and autoinhibitory domains - NMR
- 2jv3, 2kmd – mETS1 PNT domain - NMR
- 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
- 6da1, 6dat – mETS1 + SSR peptide
- Ets1 higher complexes
- 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
- 1mdm – mETS1 ETS domain + paired box protein Pax5 + MB-1 promoter DNA
- 3wu1 – hETS1 276-441 (mutant) + RUNX1 + DNA
- 3wts, 3wtt, 3wtu, 3wtv, 3wtw, 3wtx, 3wty – hETS1 276-441 (mutant) + RUNX1 + CBF beta + DNA
References
