2P6V

Structure of TAFH domain of the human TAF4 subunit of TFIID

Summary for 2P6V

• Entry DOI: 10.2210/pdb2p6v/pdb
• Descriptor: Transcription initiation factor TFIID subunit 4, SULFATE ION (3 entities in total)
• Functional Keywords: alpha helix, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O00268
• Total number of polymer chains: 1
• Total formula weight: 12747.41

Authors

Wang, X.,Truckses, D.M.,Takada, S.,Matsumura, T.,Tanese, N.,Jacobson, R.H. (deposition date: 2007-03-19, release date: 2007-05-15, Last modification date: 2025-03-26)

Primary citation

Wang, X.,Truckses, D.M.,Takada, S.,Matsumura, T.,Tanese, N.,Jacobson, R.H.
Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.
Proc.Natl.Acad.Sci.Usa, 104:7839-7844, 2007

PubMed Abstract: TBP-associated factor 4 (TAF4), an essential subunit of the TFIID complex acts as a coactivator for multiple transcriptional regulators, including Sp1 and CREB. However, little is known regarding the structural properties of the TAF4 subunit that lead to the coactivator function. Here, we report the crystal structure at 2.0-A resolution of the human TAF4-TAFH domain, a conserved domain among all metazoan TAF4, TAF4b, and ETO family members. The hTAF4-TAFH structure adopts a completely helical fold with a large hydrophobic groove that forms a binding surface for TAF4 interacting factors. Using peptide phage display, we have characterized the binding preference of the hTAF4-TAFH domain for a hydrophobic motif, DPsiPsizetazetaPsiPhi, that is present in a number of nuclear factors, including several important transcriptional regulators with roles in activating, repressing, and modulating posttranslational modifications. A comparison of the hTAF4-TAFH structure with the homologous ETO-TAFH domain reveals several critical residues important for hTAF4-TAFH target specificity and suggests that TAF4 has evolved in response to the increased transcriptional complexity of metazoans.

PubMed: 17483474
DOI: 10.1073/pnas.0608570104

Experimental method

X-RAY DIFFRACTION (2 Å)