Title : Investigation on critical structural motifs of ligands for triggering glucocorticoid receptor nuclear migration through molecular docking simulations.

Pub. Date : 2016 Jun

PMID : 26198481






7 Functional Relationships(s)
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Protein Name
Organism
1 The glucocorticoid receptor (GR), a transcription factor regulating gene expression in a ligand-dependent fashion, is known for flexibility in adapting various ligands with their structures ranging from steroid to non-steroid. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
2 The glucocorticoid receptor (GR), a transcription factor regulating gene expression in a ligand-dependent fashion, is known for flexibility in adapting various ligands with their structures ranging from steroid to non-steroid. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
3 The glucocorticoid receptor (GR), a transcription factor regulating gene expression in a ligand-dependent fashion, is known for flexibility in adapting various ligands with their structures ranging from steroid to non-steroid. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
4 The glucocorticoid receptor (GR), a transcription factor regulating gene expression in a ligand-dependent fashion, is known for flexibility in adapting various ligands with their structures ranging from steroid to non-steroid. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
5 However, in our previous study, GR shows a stringent discrimination against a set of steroid ligands with highly similar structures for triggering its nuclear migration. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
6 By analyzing the docking orientations and the related ligand-GR interaction patterns, we found that the hydrophilicity mismatch between the docking ligand and the GR ligand-binding site is the main cause combined with the steric hindrance and structural rigidness of these steroid ligands. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens
7 Furthermore, we utilized this knowledge to rationalize how the structure-binding interaction of non-steroid ligands triggers GR nuclear migration with their structures available in Protein Data Bank. Steroids nuclear receptor subfamily 3 group C member 1 Homo sapiens