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2PP4

Solution Structure of ETO-TAFH refined in explicit solvent

Summary for 2PP4
Entry DOI10.2210/pdb2pp4/pdb
NMR InformationBMRB: 7396
DescriptorProtein ETO (1 entity in total)
Functional Keywordstranscriptional cofactor, leukemia, 4-helix bundle, transcription
Biological sourceHomo sapiens (human)
Cellular locationNucleus (Potential): Q06455
Total number of polymer chains1
Total formula weight12137.99
Authors
Wei, Y.,Liu, S.,Lausen, J.,Woodrell, C.,Cho, S.,Biris, N.,Kobayashi, N.,Yokoyama, S.,Werner, M.H. (deposition date: 2007-04-27, release date: 2007-06-19, Last modification date: 2024-05-22)
Primary citationWei, Y.,Liu, S.,Lausen, J.,Woodrell, C.,Cho, S.,Biris, N.,Kobayashi, N.,Wei, Y.,Yokoyama, S.,Werner, M.H.
A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription
Nat.Struct.Mol.Biol., 14:653-661, 2007
Cited by
PubMed Abstract: The eight twenty-one protein, ETO, is implicated in 12%-15% of acute human leukemias as part of a gene fusion with RUNX1 (also called AML1). Of the four ETO domains related to Drosophila melanogaster Nervy, only two are required to induce spontaneous myeloid leukemia upon transplantation into the mouse. One of these domains is related in sequence to TAF4, a component of TFIID. The structure of this domain, ETO-TAFH, is similar to yeast Rpb4 and to Escherichia coli sigma(70); it is the first TAF-related protein with structural similarity to the multisubunit RNA polymerases. Overlapping surfaces of ETO-TAFH interact with an autonomous repression domain of the nuclear receptor corepressor N-CoR and with a conserved activation domain from the E-box family of transcription factors. Thus, ETO-TAFH acts as a structural platform that can interchange negative and positive coregulatory proteins to control transcription.
PubMed: 17572682
DOI: 10.1038/nsmb1258
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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