الفهرس 
Introduction and Aim of The WorkOnly 14 pages are availabe for public view
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Abstract
In our study, using the bacterial expression system , we were able to identify that the dimerization domain of progesterone receptor is localized in the c-terminal 164 amino acids of ligand binding domain. This expressed fragment of hpR was able to dimerze to itself (homodimerization) as well as to the full length receptor present in the extract of the breast cancer cells T47D (heterodimerization) . this concludes that we have identified a dimerization domain in that portion of the human progesterone receptor (hpR) and it can carry out the dimerization function away from the rest of the receptor molecule. To limit the number of amino acids responsible this dimerization function