Eukaryotic transcription factors.
Recently determined high-resolution structures of eukaryotic transcription factors have illuminated the enzymatic mechanism underlying transcription. Progress has been made in characterising protein-protein interactions between negative cofactors and general transcription factors, and between transrepression domains and corepressors. Structures of sequence-specific transcription factors have revealed further versatility in the mode of interaction with DNA and several have provided new insights into the molecular basis of human disease.
Warren
Alan J
AJ
MRC Laboratory of Molecular Biology, Hills Road, CB22QH, Cambridge, UK ajw@mrc-lmb.cam.ac.uk
D019175:DNA Methylation; D005057:Eukaryotic Cells; D005786:Gene Expression Regulation; D019077:Helix-Turn-Helix Motifs / Q000502:physiology; D006801:Humans; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D035362:Transcription Factor TFIID; D051758:Transcription Factor TFIIH; D014157:Transcription Factors / Q000737:chemistry* / Q000502:physiology*; D019473:Transcription Factors, TFII / Q000502:physiology; D014158:Transcription, Genetic; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000502:physiology
D035362:Transcription Factor TFIID; D014157:Transcription Factors; D019473:Transcription Factors, TFII; D016159:Tumor Suppressor Protein p53; D051758:Transcription Factor TFIIH