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2p6v

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Revision as of 13:05, 23 January 2008 by OCA (Talk | contribs)
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Image:2p6v.gif

2p6v, resolution 2.00Å

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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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