Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
DNA Methylation
-
Eukaryotic Cells
-
Gene Expression Regulation
-
Helix-Turn-Helix Motifs / physiology
-
Humans
-
Protein Conformation
-
Structure-Activity Relationship
-
Transcription Factor TFIID
-
Transcription Factor TFIIH
-
Transcription Factors / chemistry*
-
Transcription Factors / physiology*
-
Transcription Factors, TFII / physiology
-
Transcription, Genetic
-
Tumor Suppressor Protein p53 / chemistry
-
Tumor Suppressor Protein p53 / physiology
Substances
-
Transcription Factor TFIID
-
Transcription Factors
-
Transcription Factors, TFII
-
Tumor Suppressor Protein p53
-
Transcription Factor TFIIH