http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2007111265-A1
Outgoing Links
Predicate | Object |
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assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_aa1f97d963ba8d6d4c8acc88be41cbb8 |
classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-566 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G06F19-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-567 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K31-573 |
filingDate | 2006-11-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7a10f90d2493a0a7a4062f1fe8e0ef29 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_dead7250e765b49dd1da867998b49576 |
publicationDate | 2007-05-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | US-2007111265-A1 |
titleOfInvention | Ligands for mineralocorticoid receptor (MR) and methods for screening for or designing MR ligands |
abstract | The inventors disclose a 1.95 Å crystal structure of the MR ligand binding domain containing a single C808S mutation bound to a corticosterone and the fourth LXXLL motif of steroid receptor coactivator-1 (SRC1-4). The inventors demonstrate that SRC1-4 is the most potent MR-binding motif and mutations that disrupt the MR/SRC1-4 interactions abolish the ability of the full-length SRC1 to coactivate MR. The structure also reveals a compact steroid binding pocket with a unique topology that is primarily defined by key residues of helices 6 and 7. Also described are novel ligands for MR, methods for screening for and designing novel MR ligands, and methods for treating MR-related diseases. |
isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2007219348-A1 |
priorityDate | 2005-11-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 244.