2p6v
From Proteopedia
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==Overview== | ==Overview== | ||
| - | TBP-associated factor 4 (TAF4), an essential subunit of the TFIID complex | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jacobson, R | + | [[Category: Jacobson, R H.]] |
[[Category: Matsumura, T.]] | [[Category: Matsumura, T.]] | ||
[[Category: Takada, S.]] | [[Category: Takada, S.]] | ||
[[Category: Tanese, N.]] | [[Category: Tanese, N.]] | ||
| - | [[Category: Truckses, D | + | [[Category: Truckses, D M.]] |
[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:26:28 2008'' |
Revision as of 16:26, 21 February 2008
|
Structure of TAFH domain of the human TAF4 subunit of TFIID
Overview
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.
About this Structure
2P6V is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators., Wang X, Truckses DM, Takada S, Matsumura T, Tanese N, Jacobson RH, Proc Natl Acad Sci U S A. 2007 May 8;104(19):7839-44. Epub 2007 May 1. PMID:17483474
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