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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2010
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| 008 | 190411s2010 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-77951762462 | |
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| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Veleiro, A.S. | |
| 245 | 1 | 0 | |a Structure of the glucocorticoid receptor, a flexible protein that can adapt to different ligands |
| 260 | |c 2010 | ||
| 270 | 1 | 0 | |m Burton, G.; Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Universidad de Buenos Aires, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina; email: burton@qo.fcen.uba.ar |
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| 520 | 3 | |a 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. |l eng | |
| 593 | |a Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Universidad de Buenos Aires, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a GLUCOCORTICOIDS |
| 690 | 1 | 0 | |a HORMONES |
| 690 | 1 | 0 | |a NUCLEAR RECEPTORS |
| 690 | 1 | 0 | |a PROTEIN STRUCTURES |
| 690 | 1 | 0 | |a STEROIDS |
| 690 | 1 | 0 | |a ALDOSTERONE |
| 690 | 1 | 0 | |a DEACYLCORTIVAZOL |
| 690 | 1 | 0 | |a DEOXYCORTICOSTERONE |
| 690 | 1 | 0 | |a DEXAMETHASONE |
| 690 | 1 | 0 | |a DIMER |
| 690 | 1 | 0 | |a FLUTICASONE FUROATE |
| 690 | 1 | 0 | |a FLUTICASONE PROPIONATE |
| 690 | 1 | 0 | |a GLUCOCORTICOID |
| 690 | 1 | 0 | |a GLUCOCORTICOID RECEPTOR |
| 690 | 1 | 0 | |a GLUCOCORTICOID RECEPTOR ANTAGONIST |
| 690 | 1 | 0 | |a HYDROCORTISONE |
| 690 | 1 | 0 | |a LIGAND |
| 690 | 1 | 0 | |a MIFEPRISTONE |
| 690 | 1 | 0 | |a NUCLEAR RECEPTOR COACTIVATOR 2 |
| 690 | 1 | 0 | |a STEROID |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a AGONIST |
| 690 | 1 | 0 | |a AMINO TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ANTIINFLAMMATORY ACTIVITY |
| 690 | 1 | 0 | |a APOPTOSIS |
| 690 | 1 | 0 | |a ASTHMA |
| 690 | 1 | 0 | |a AUTOIMMUNE DISEASE |
| 690 | 1 | 0 | |a BINDING SITE |
| 690 | 1 | 0 | |a CARBOXY TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a CONFORMATION |
| 690 | 1 | 0 | |a CRYSTAL STRUCTURE |
| 690 | 1 | 0 | |a DERMATITIS |
| 690 | 1 | 0 | |a DIABETES MELLITUS |
| 690 | 1 | 0 | |a DRUG MECHANISM |
| 690 | 1 | 0 | |a DRUG RECEPTOR BINDING |
| 690 | 1 | 0 | |a GENE MUTATION |
| 690 | 1 | 0 | |a HYDROPHILICITY |
| 690 | 1 | 0 | |a HYDROPHOBICITY |
| 690 | 1 | 0 | |a HYPERTENSION |
| 690 | 1 | 0 | |a IMMUNOREGULATION |
| 690 | 1 | 0 | |a IMMUNOSUPPRESSIVE TREATMENT |
| 690 | 1 | 0 | |a LEUKEMIA |
| 690 | 1 | 0 | |a LIGAND BINDING |
| 690 | 1 | 0 | |a LYMPHOMA |
| 690 | 1 | 0 | |a MOLECULAR INTERACTION |
| 690 | 1 | 0 | |a MOLECULAR RECOGNITION |
| 690 | 1 | 0 | |a MYELOMA |
| 690 | 1 | 0 | |a OBESITY |
| 690 | 1 | 0 | |a OSTEOPOROSIS |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a PROTEIN MOTIF |
| 690 | 1 | 0 | |a PROTEIN PROTEIN INTERACTION |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a RHEUMATOID ARTHRITIS |
| 690 | 1 | 0 | |a SHORT SURVEY |
| 690 | 1 | 0 | |a BINDING SITES |
| 690 | 1 | 0 | |a COMPUTER SIMULATION |
| 690 | 1 | 0 | |a CRYSTALLOGRAPHY, X-RAY |
| 690 | 1 | 0 | |a LIGANDS |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE, TERTIARY |
| 690 | 1 | 0 | |a RECEPTORS, GLUCOCORTICOID |
| 653 | 0 | 0 | |a ru 486 |
| 700 | 1 | |a Alvarez, L.D. | |
| 700 | 1 | |a Eduardo, S.L. | |
| 700 | 1 | |a Burton, G. | |
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| 856 | 4 | 0 | |u https://doi.org/10.1002/cmdc.201000014 |y DOI |
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