3B5R
Crystal structure of the androgen receptor ligand binding domain in complex with SARM C-31
Summary for 3B5R
| Entry DOI | 10.2210/pdb3b5r/pdb |
| Related | 2axa 3B65 3B66 3B67 3B68 |
| Descriptor | Androgen receptor, (2S)-3-(4-chloro-3-fluorophenoxy)-N-[4-cyano-3-(trifluoromethyl)phenyl]-2-hydroxy-2-methylpropanamide (3 entities in total) |
| Functional Keywords | androgen receptor, nonsteroidal, sarm, disease mutation, dna-binding, lipid-binding, metal-binding, nucleus, polymorphism, steroid-binding, transcription, transcription regulation, triplet repeat expansion, ubl conjugation, zinc, zinc-finger |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus: P10275 |
| Total number of polymer chains | 1 |
| Total formula weight | 29462.83 |
| Authors | Bohl, C.E.,Miller, D.D.,Dalton, J.T. (deposition date: 2007-10-26, release date: 2008-09-09, Last modification date: 2024-02-21) |
| Primary citation | Bohl, C.E.,Wu, Z.,Chen, J.,Mohler, M.L.,Yang, J.,Hwang, D.J.,Mustafa, S.,Miller, D.D.,Bell, C.E.,Dalton, J.T. Effect of B-ring substitution pattern on binding mode of propionamide selective androgen receptor modulators Bioorg.Med.Chem.Lett., 18:5567-5570, 2008 Cited by PubMed Abstract: Selective androgen receptor modulators (SARMs) are essentially prostate sparing androgens, which provide therapeutic potential in osteoporosis, male hormone replacement, and muscle wasting. Herein we report crystal structures of the androgen receptor (AR) ligand-binding domain (LBD) complexed to a series of potent synthetic nonsteroidal SARMs with a substituted pendant arene referred to as the B-ring. We found that hydrophilic B-ring para-substituted analogs exhibit an additional region of hydrogen bonding not seen with steroidal compounds and that multiple halogen substitutions affect the B-ring conformation and aromatic interactions with Trp741. This information elucidates interactions important for high AR binding affinity and provides new insight for structure-based drug design. PubMed: 18805694DOI: 10.1016/j.bmcl.2008.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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