Abstract
Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.
Original language | English (US) |
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Pages (from-to) | 591-597 |
Number of pages | 7 |
Journal | Nature |
Volume | 327 |
Issue number | 6123 |
DOIs | |
State | Published - 1987 |
ASJC Scopus subject areas
- General