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A metal‐linked gapped zipper model is proposed for theh sp90‐glucocorticoid receptor interaction
Author(s) -
Schwartz J.A.,
Mizukami H.,
Skafar D.F.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81144-o
Subject(s) - leucine zipper , glucocorticoid receptor , hsp90 , chemistry , biophysics , heat shock protein , binding site , binding domain , plasma protein binding , zipper , biochemistry , receptor , microbiology and biotechnology , biology , transcription factor , computer science , gene , algorithm
In the presence of certain metals, regions of the hormone binding domain of the glucocorticoid receptor (GR) are capable of binding the 90 kDa heat shock protein (hsp90). Using secondary structure prediction methods in correlation with the experimental data, we propose a model which predicts the presence of two widely spaced leucine zipper‐like heptads on either side of a central subdomain. The heptads could interact hydrophobically with similar regions on the hsp90 homodimer, bringing putative metal binding residues on each protein close enough to establish a shared metal bridge. The central subdomain between heptads is suggested to contain regions involved in metal binding, steroid binding, and conformational mobility. The hypothetical model that we are proposing therefore addresses the nature of the structural link between hsp90 binding, hormone binding, and conformational changes in the receptor.