Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands
Crystal structures of the glucocorticoid receptor (GR) ligand binding domain in complex with various agonists and antagonists give us an insight on how ligands are recognized by the receptor and how their structure can affect the behavior of the GR. Interestingly, these structural data show how the...
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todo:paper_18607179_v5_n5_p649_Veleiro2023-10-03T16:33:21Z Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands Veleiro, A.S. Alvarez, L.D. Eduardo, S.L. Burton, G. Glucocorticoids Hormones Nuclear receptors Protein structures Steroids aldosterone deacylcortivazol deoxycorticosterone dexamethasone dimer fluticasone furoate fluticasone propionate glucocorticoid glucocorticoid receptor glucocorticoid receptor antagonist hydrocortisone ligand mifepristone nuclear receptor coactivator 2 steroid unclassified drug agonist amino terminal sequence antiinflammatory activity apoptosis asthma autoimmune disease binding site carboxy terminal sequence conformation crystal structure dermatitis diabetes mellitus drug mechanism drug receptor binding gene mutation hydrophilicity hydrophobicity hypertension immunoregulation immunosuppressive treatment leukemia ligand binding lymphoma molecular interaction molecular recognition myeloma obesity osteoporosis priority journal protein binding protein motif protein protein interaction protein structure rheumatoid arthritis short survey Binding Sites Computer Simulation Crystallography, X-Ray Ligands Protein Structure, Tertiary Receptors, Glucocorticoid Crystal structures of the glucocorticoid receptor (GR) ligand binding domain in complex with various agonists and antagonists give us an insight on how ligands are recognized by the receptor and how their structure can affect the behavior of the GR. Interestingly, these structural data show how the GR can adapt its binding pocket to accommodate molecules that differ substantially from the natural ligands without loss of function. (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KGaA. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_18607179_v5_n5_p649_Veleiro |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Glucocorticoids Hormones Nuclear receptors Protein structures Steroids aldosterone deacylcortivazol deoxycorticosterone dexamethasone dimer fluticasone furoate fluticasone propionate glucocorticoid glucocorticoid receptor glucocorticoid receptor antagonist hydrocortisone ligand mifepristone nuclear receptor coactivator 2 steroid unclassified drug agonist amino terminal sequence antiinflammatory activity apoptosis asthma autoimmune disease binding site carboxy terminal sequence conformation crystal structure dermatitis diabetes mellitus drug mechanism drug receptor binding gene mutation hydrophilicity hydrophobicity hypertension immunoregulation immunosuppressive treatment leukemia ligand binding lymphoma molecular interaction molecular recognition myeloma obesity osteoporosis priority journal protein binding protein motif protein protein interaction protein structure rheumatoid arthritis short survey Binding Sites Computer Simulation Crystallography, X-Ray Ligands Protein Structure, Tertiary Receptors, Glucocorticoid |
| spellingShingle |
Glucocorticoids Hormones Nuclear receptors Protein structures Steroids aldosterone deacylcortivazol deoxycorticosterone dexamethasone dimer fluticasone furoate fluticasone propionate glucocorticoid glucocorticoid receptor glucocorticoid receptor antagonist hydrocortisone ligand mifepristone nuclear receptor coactivator 2 steroid unclassified drug agonist amino terminal sequence antiinflammatory activity apoptosis asthma autoimmune disease binding site carboxy terminal sequence conformation crystal structure dermatitis diabetes mellitus drug mechanism drug receptor binding gene mutation hydrophilicity hydrophobicity hypertension immunoregulation immunosuppressive treatment leukemia ligand binding lymphoma molecular interaction molecular recognition myeloma obesity osteoporosis priority journal protein binding protein motif protein protein interaction protein structure rheumatoid arthritis short survey Binding Sites Computer Simulation Crystallography, X-Ray Ligands Protein Structure, Tertiary Receptors, Glucocorticoid Veleiro, A.S. Alvarez, L.D. Eduardo, S.L. Burton, G. Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| topic_facet |
Glucocorticoids Hormones Nuclear receptors Protein structures Steroids aldosterone deacylcortivazol deoxycorticosterone dexamethasone dimer fluticasone furoate fluticasone propionate glucocorticoid glucocorticoid receptor glucocorticoid receptor antagonist hydrocortisone ligand mifepristone nuclear receptor coactivator 2 steroid unclassified drug agonist amino terminal sequence antiinflammatory activity apoptosis asthma autoimmune disease binding site carboxy terminal sequence conformation crystal structure dermatitis diabetes mellitus drug mechanism drug receptor binding gene mutation hydrophilicity hydrophobicity hypertension immunoregulation immunosuppressive treatment leukemia ligand binding lymphoma molecular interaction molecular recognition myeloma obesity osteoporosis priority journal protein binding protein motif protein protein interaction protein structure rheumatoid arthritis short survey Binding Sites Computer Simulation Crystallography, X-Ray Ligands Protein Structure, Tertiary Receptors, Glucocorticoid |
| description |
Crystal structures of the glucocorticoid receptor (GR) ligand binding domain in complex with various agonists and antagonists give us an insight on how ligands are recognized by the receptor and how their structure can affect the behavior of the GR. Interestingly, these structural data show how the GR can adapt its binding pocket to accommodate molecules that differ substantially from the natural ligands without loss of function. (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KGaA. |
| format |
JOUR |
| author |
Veleiro, A.S. Alvarez, L.D. Eduardo, S.L. Burton, G. |
| author_facet |
Veleiro, A.S. Alvarez, L.D. Eduardo, S.L. Burton, G. |
| author_sort |
Veleiro, A.S. |
| title |
Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| title_short |
Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| title_full |
Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| title_fullStr |
Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| title_full_unstemmed |
Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| title_sort |
structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| url |
http://hdl.handle.net/20.500.12110/paper_18607179_v5_n5_p649_Veleiro |
| work_keys_str_mv |
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| _version_ |
1782029552638230528 |