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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The three-dimensional structure of trp repressor.

The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface.[1]

References

  1. The three-dimensional structure of trp repressor. Schevitz, R.W., Otwinowski, Z., Joachimiak, A., Lawson, C.L., Sigler, P.B. Nature (1985) [Pubmed]
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