Impaired helix 12 dynamics due to proline 892 substitutions in the androgen receptor are associated with complete androgen insensitivity

Structural studies of the ligand-binding domain (LBD) of several steroid receptors have revealed that the dynamic properties of the C-terminal helix 12 (H12) are the major determinant of the activation mode of these receptors. H12 exhibits high mobility and different conformations in the absence of...

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Veröffentlicht in:	Human molecular genetics 2006-03, Vol.15 (6), p.921-931
Hauptverfasser:	Elhaji, Youssef A., Stoica, Ileana, Dennis, Sheldon, Purisima, Enrico O., Trifiro, Mark A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution - genetics Androgen-Insensitivity Syndrome - diagnosis Androgen-Insensitivity Syndrome - genetics Androgen-Insensitivity Syndrome - metabolism Animals Biological and medical sciences Cell receptors Cell structures and functions Cells, Cultured Cercopithecus aethiops COS Cells DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Female Fibroblasts - metabolism Fibroblasts - pathology Fundamental and applied biological sciences. Psychology Genetics of eukaryotes. Biological and molecular evolution Humans Ligands Male Miscellaneous Molecular and cellular biology Molecular Sequence Data Mutation Proline - genetics Protein Binding - genetics Protein Structure, Secondary - genetics Protein Structure, Tertiary - genetics Receptors, Androgen - chemistry Receptors, Androgen - genetics Receptors, Androgen - metabolism Thermodynamics
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