2p6v: Difference between revisions
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|PDB= 2p6v |SIZE=350|CAPTION= <scene name='initialview01'>2p6v</scene>, resolution 2.00Å | |PDB= 2p6v |SIZE=350|CAPTION= <scene name='initialview01'>2p6v</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6v OCA], [http://www.ebi.ac.uk/pdbsum/2p6v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p6v RCSB]</span> | |||
}} | }} | ||
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[[Category: Truckses, D M.]] | [[Category: Truckses, D M.]] | ||
[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
[[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 Mon Mar 31 04:31:03 2008'' | ||
Revision as of 01:31, 31 March 2008
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| 2p6v, resolution 2.00Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | MLY, SO4 | ||||||||||||
| Gene: | TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 (Homo sapiens) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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