Characterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI).

ABSTRACT:

Background

Earlier studies showed that 17β-estradiol (E(2)), an endogenous female sex hormone, can bind to human protein disulfide isomerase (PDI), a protein folding catalyst for disulfide bond formation and rearrangement. This binding interaction can modulate the intracellular levels of E(2) and its biological actions. However, the structure of PDI's E(2)-binding site is still unclear at present, which is the focus of this study.

Methodology/principal findings

The E(2)-binding site structure of human PDI was studied by using various biochemical approaches coupled with radiometric receptor-binding assays, site-directed mutagenesis, and molecular computational modeling. Analysis of various PDI protein fragments showed that the [(3)H]E(2)-binding activity is not associated wit

SUBMITTER: Fu XM 

PROVIDER: S-EPMC3207843 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature