Abstract
We report cDNA sequence, the complete derived as sequence, and a predicted secondary structure of the chick hsp 90, a protein which has been found to form complexes with steroid hormone receptors. The modelling of the most negatively charged “region A” indicates that the α-helices of this portion of hsp 90 minick DNA configuration. We propose that this region can, in absence of hormone, interact with and cap the positively charged DNA-binding domain of steroid receptors.
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