1sr7: Difference between revisions
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|PDB= 1sr7 |SIZE=350|CAPTION= <scene name='initialview01'>1sr7</scene>, resolution 1.46Å | |PDB= 1sr7 |SIZE=350|CAPTION= <scene name='initialview01'>1sr7</scene>, resolution 1.46Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MOF:MOMETASONE+FUROATE'>MOF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PGR, NR3C3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PGR, NR3C3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1a28|1A28]], [[1e3k|1E3K]], [[1sqn|1SQN]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr7 OCA], [http://www.ebi.ac.uk/pdbsum/1sr7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sr7 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: hormone receptor]] | [[Category: hormone receptor]] | ||
[[Category: mometasone]] | [[Category: mometasone]] | ||
| Line 44: | Line 41: | ||
[[Category: progesterone receptor]] | [[Category: progesterone 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 23:46:01 2008'' | ||
Revision as of 23:46, 30 March 2008
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| , resolution 1.46Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | PGR, NR3C3 (Homo sapiens) | ||||||
| Related: | 1A28, 1E3K, 1SQN
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Progesterone Receptor Hormone Binding Domain with Bound Mometasone Furoate
OverviewOverview
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 StructureAbout this Structure
1SR7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Progesterone receptor ligand binding pocket flexibility: crystal structures of the norethindrone and mometasone furoate complexes., Madauss KP, Deng SJ, Austin RJ, Lambert MH, McLay I, Pritchard J, Short SA, Stewart EL, Uings IJ, Williams SP, J Med Chem. 2004 Jun 17;47(13):3381-7. PMID:15189034
Page seeded by OCA on Sun Mar 30 23:46:01 2008