1sqn: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= HUMPGRR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= HUMPGRR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1a28|1A28]], [[1e3k|1E3K]], [[1zyx|1ZYX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqn OCA], [http://www.ebi.ac.uk/pdbsum/1sqn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sqn RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Although progesterone, the natural ligand of the progesterone receptor (PR), has a hydrogen atom at the 17alpha position, other potent steroid agonists such as norethindrone and mometasone furoate have larger substituents at this position that are accommodated by the PR ligand binding pocket. Crystallographic analysis of PR ligand binding domain complexes clearly demonstrated that these moieties were accommodated by local shifts of the protein main chain and by adoption of alternative side chain rotamer conformations of ligand-proximal amino acids. These conformational changes imparted a ligand-specific volume to the binding pocket, from 490 A3 in the metribolone complex to 520 A3 in the norethindrone complex, 565 A3 in the progesterone complex, and 730 A3 in the mometasone furoate complex. Despite these marked alterations in binding pocket volume, critical interactions essential for establishment of an active AF2 conformation were maintained. | Although progesterone, the natural ligand of the progesterone receptor (PR), has a hydrogen atom at the 17alpha position, other potent steroid agonists such as norethindrone and mometasone furoate have larger substituents at this position that are accommodated by the PR ligand binding pocket. Crystallographic analysis of PR ligand binding domain complexes clearly demonstrated that these moieties were accommodated by local shifts of the protein main chain and by adoption of alternative side chain rotamer conformations of ligand-proximal amino acids. These conformational changes imparted a ligand-specific volume to the binding pocket, from 490 A3 in the metribolone complex to 520 A3 in the norethindrone complex, 565 A3 in the progesterone complex, and 730 A3 in the mometasone furoate complex. Despite these marked alterations in binding pocket volume, critical interactions essential for establishment of an active AF2 conformation were maintained. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Uings, I J.]] | [[Category: Uings, I J.]] | ||
[[Category: Williams, S P.]] | [[Category: Williams, S P.]] | ||
[[Category: | [[Category: birth control]] | ||
[[Category: progesterone receptor | [[Category: norethindrone]] | ||
[[Category: nuclear receptor]] | |||
[[Category: progesterone receptor]] | |||
[[Category: steroid receptor]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:41 2008'' | ||
