作者: Catherine Birck , Olivier Poch , Christophe Romier , Marc Ruff , Gabrielle Mengus
DOI: 10.1016/S0092-8674(00)81423-3
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摘要: Abstract Determination of the crystal structure human TBP-associated factor (hTAF II )28/hTAF 18 heterodimer shows that these TAF s form a novel histone-like pair in TFIID complex. The histone folds hTAF 28 and were not predicted from their primary sequence, indicating define family atypical fold sequences. motifs are also present N- C-terminal regions SPT3 proteins, suggesting may be reconstituted by intramolecular rather than classical intermolecular interactions. existence additional pairs both SAGA complexes is more commonly used motif for mediating TAF–TAF interactions previously believed.