1bh9: Difference between revisions

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[[Image:1bh9.gif|left|200px]]
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{{STRUCTURE_1bh9|  PDB=1bh9  |  SCENE=  }}  
{{STRUCTURE_1bh9|  PDB=1bh9  |  SCENE=  }}  


'''HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS'''
===HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS===




==Overview==
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Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed.
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==About this Structure==
==About this Structure==
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[[Category: Tata binding protein]]
[[Category: Tata binding protein]]
[[Category: Transcription regulation complex]]
[[Category: Transcription regulation complex]]
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Revision as of 19:09, 30 June 2008

File:1bh9.png

Template:STRUCTURE 1bh9

HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBSHTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS

Template:ABSTRACT PUBMED 9695952

About this StructureAbout this Structure

1BH9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family., Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D, Cell. 1998 Jul 24;94(2):239-49. PMID:9695952

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