1tba
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(New page: 200px<br /><applet load="1tba" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tba" /> '''SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX...)
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Revision as of 01:00, 21 November 2007
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SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX: PROTEIN MIMICRY OF THE MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND BY TBP, NMR, 25 STRUCTURES
Overview
General transcription factor TFIID consists of TATA box-binding protein, (TBP) and TBP-associated factors (TAF(II)s), which together play a central, role in both positive and negative regulation of transcription. The, N-terminal region of the 230 kDa Drosophila TAF(II) (dTAF(II)230) binds, directly to TBP and inhibits TBP binding to the TATA box. We report here, the solution structure of the complex formed by dTAF(II)230 N-terminal, region (residues 11-77) and TBP. dTAF(II)230(11-77) comprises three alpha, helices and a beta hairpin, forming a core that occupies the concave, DNA-binding surface of TBP. The TBP-binding surface of dTAF(II)230, markedly resembles the minor groove surface of the partially unwound TATA, box in the TBP-TATA complex. This protein mimicry of the TATA element, surface provides the structural basis of the mechanism by which, dTAF(II)230 negatively controls the TATA box-binding activity within the, TFIID complex.
About this Structure
1TBA is a Protein complex structure of sequences from Drosophila melanogaster and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP., Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M, Cell. 1998 Sep 4;94(5):573-83. PMID:9741622
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