2nxp
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(New page: 200px<br /> <applet load="2nxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nxp, resolution 2.17Å" /> '''Structure of NTD2 d...)
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Revision as of 20:57, 12 November 2007
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Structure of NTD2 domain of the human TAF5 subunit of TFIID
Overview
TFIID is an essential factor required for RNA polymerase II transcription, but remains poorly understood because of its intrinsic complexity. Human, TAF5, a 100-kDa subunit of general transcription factor TFIID, is an, essential gene and plays a critical role in assembling the 1.2 MDa TFIID, complex. We report here a structural analysis of the TAF5 protein. Our, structure at 2.2-A resolution of the TAF5-NTD2 domain reveals an, alpha-helical domain with distant structural similarity to RNA polymerase, II CTD interacting factors. The TAF5-NTD2 domain contains several, conserved clefts likely to be critical for TFIID complex assembly. Our, biochemical analysis of the human TAF5 protein demonstrates the ability of, the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a, key property required for the assembly of the TFIID complex.
About this Structure
2NXP is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural analysis and dimerization potential of the human TAF5 subunit of TFIID., Bhattacharya S, Takada S, Jacobson RH, Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1189-94. Epub 2007 Jan 16. PMID:17227857
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