hdl:10101/npre.2009.3316.1
6 votes
Document Type:
Manuscript
Date:
Received 03 June 2009 21:14 UTC; Posted 05 June 2009
Subjects:
Cancer, Developmental Biology, Bioinformatics, Evolutionary Biology
Tags:
Abstract:

The origins of signaling by vertebrate steroids are not fully understood. An important advance was the report that an estrogen-binding steroid receptor [SR] is present in amphioxus, a basal chordate with a similar body plan as vertebrates. To investigate the evolution of estrogen binding to steroid receptors, we constructed a 3D model of amphioxus SR complexed with estradiol. This 3D model indicates that although the SR is activated by estradiol, some interactions between estradiol and human ERα are not conserved in the SR, which can explain the low affinity of estradiol for the SR. These differences between the SR and ERα in the steroid-binding domain are sufficient to suggest that another steroid is the physiological regulator of the SR. The 3D model predicts that mutation of Glu-346 to Gln will increase the affinity of testosterone for amphioxus SR and elucidate the evolution of steroid binding to nuclear receptors.

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This document is licensed to the public under the Creative Commons Attribution 3.0 License
How to cite this document:

Baker, Michael and Chang, David. 3D model of amphioxus steroid receptor complexed with estradiol. Available from Nature Precedings <http://hdl.handle.net/10101/npre.2009.3316.1> (2009)

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