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Full-Text Articles in Physical Sciences and Mathematics
Unbinding Of Testosterone From The Androgen Receptor And Two Bf-3 Site Mutants, Muniruzzaman Chowdhury
Unbinding Of Testosterone From The Androgen Receptor And Two Bf-3 Site Mutants, Muniruzzaman Chowdhury
Theses and Dissertations
The androgen receptor (AR) can be activated by molecules binding in the steroid binding pocket. It can also be regulated allosterically by cofactors binding to the AF-2 surface site as well as by exogenous small molecules binding to the BF-3 surface site. Recent data indicated that mutations in the BF-3 site changed the amount of the endogenous steroid needed to activate the receptor, indicating that mutations of BF-3 can cause an allosteric effect. Molecular dynamics and steered molecular dynamics simulations were used to study the allosteric effect of the mutations on AR structure and the unbinding pathways of testosterone (TES) …
Studies On Regulation Of Dihydrotestosterone Binding To And Releasing From The Androgen Receptor, Tahyra M. Resto Santos
Studies On Regulation Of Dihydrotestosterone Binding To And Releasing From The Androgen Receptor, Tahyra M. Resto Santos
Theses and Dissertations
The androgen receptor (AR) is a nuclear receptor that responds to testosterone and 5α-dihydrotestosterone (DHT) by modulating gene expression in a variety of cells, including prostate and muscle tissues. Studies of small molecule interaction with AR have shown diphenyl compounds inhibiting through a binding site labeled Binding Function 3 (BF3). The goal of this research is to analyze the interaction of the BF3 site with DDT and related compounds. Amino acids that are exposed on the surface of the BF3 that might interact with different compounds were mutated. Mutant proteins were tested experimentally for their impact on the inhibition the …