International Journal of Molecular Medical Science, 2024, Vol.14, No.1, 24-28 http://medscipublisher.com/index.php/ijmms 25 Figure 1 Diverse action mechanisms of the glucocorticoid receptor (GR) Figure 2 shows the isomeric communication within the glucocorticoid receptor (GR) structure and its new dimeric interface. GR consists of four structural domains: N-terminal domain (NTD), DNA binding domain (DBD), hinge region (HR), and ligand binding domain (LBD). DNA is considered an isomeric regulator of DBD conformation. Similarly, the binding of different ligands and co modulators also alters the conformation of LBD in different ways. In LBD, there are ligand and co regulatory binding pockets, and there is bidirectional communication between them. In addition, after ligand binding, domain to domain communication also occurs from LBD to DBD. The repositioning of the R611 site has expanded the pocket size, allowing for the binding of larger molecules. The A458 (DBD) and I628 (LBD) residues are crucial at the dimer interface, and dual mutations can lead to complete loss of function. The newly proposed LBD dimer exhibits a head to tail structure. There are still doubts about higher-level oligomeric states of GR (such as tetramers or higher), but a possible explanation is that they aggregate distant glucocorticoid binding sequences (GBSs) together. Figure 2 Allosteric communication within the GR structure and its new dimer interface
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