David Auble
Here you can view the solution structure of the HMG domain of human SRY (green) bound to DNA (blue; 1hry). SRY is a transcription factor involved in the initiation of male sex determination, and has been described as having a twisted L shape. Three alpha helices are arranged to create a concave DNA binding surface for interaction with the minor groove. The DNA is greatly distorted in the complex: it is underwound and bent ~70-80 degrees. While the structure of SRY is completely different from that of TBP, these two proteins are similar in using a hydrophobic DNA binding pocket to interact with a splayed and bent minor groove. As the interaction occurs exclusively via the minor groove, not surprisingly, there are few hydrogen bonds with the base edges.
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