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[[ | ==STRUCTURAL BASIS FOR AGONISM AND ANTAGONISM FOR A SET OF CHEMICALLY RELATED PROGESTERONE RECEPTOR MODULATORS== | ||
<StructureSection load='3zrb' size='340' side='right' caption='[[3zrb]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zrb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZRB FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OR8:2-CHLORO-N-[[4-(3,5-DIMETHYLISOXAZOL-4-YL)PHENYL]METHYL]-1,4-DIMETHYL-1H-PYRAZOLE-4-SULFONAMIDE'>OR8</scene>, <scene name='pdbligand=ORC:(R)-N-[1-[4-(3,5-DIMETHYLISOXAZOL-4-YL)PHENYL]ETHYL]-3,5-DIMETHYLISOXAZOLE-4-SULFONAMIDE'>ORC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c7a|2c7a]], [[2w8y|2w8y]], [[1a28|1a28]], [[1zuc|1zuc]], [[3zr7|3zr7]], [[1sqn|1sqn]], [[1sr7|1sr7]], [[1e3k|1e3k]], [[3zra|3zra]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zrb RCSB], [http://www.ebi.ac.uk/pdbsum/3zrb PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The progesterone receptor is able to bind to a large number and variety of ligands that elicit a broad range of transcriptional responses ranging from full agonism to full antagonism and numerous mixed profiles inbetween. We describe here two new progesterone receptor ligand binding domain x-ray structures bound to compounds from a structurally related but functionally divergent series, which show different binding modes corresponding to their agonistic or antagonistic nature. In addition, we present a third progesterone receptor ligand binding domain dimer bound to an agonist in monomer A and an antagonist in monomer B, which display binding modes in agreement with the earlier observation that agonists and antagonists from this series adopt different binding modes. | |||
Structural basis for agonism and antagonism for a set of chemically related progesterone receptor modulators.,Lusher SJ, Raaijmakers HC, Vu-Pham D, Dechering K, Lam TW, Brown AR, Hamilton NM, Nimz O, Bosch R, McGuire R, Oubrie A, de Vlieg J J Biol Chem. 2011 Oct 7;286(40):35079-86. Epub 2011 Aug 17. PMID:21849509<ref>PMID:21849509</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Azevedo, R.]] | [[Category: Azevedo, R.]] | ||
Revision as of 11:32, 5 June 2014
STRUCTURAL BASIS FOR AGONISM AND ANTAGONISM FOR A SET OF CHEMICALLY RELATED PROGESTERONE RECEPTOR MODULATORSSTRUCTURAL BASIS FOR AGONISM AND ANTAGONISM FOR A SET OF CHEMICALLY RELATED PROGESTERONE RECEPTOR MODULATORS
Structural highlights
Publication Abstract from PubMedThe progesterone receptor is able to bind to a large number and variety of ligands that elicit a broad range of transcriptional responses ranging from full agonism to full antagonism and numerous mixed profiles inbetween. We describe here two new progesterone receptor ligand binding domain x-ray structures bound to compounds from a structurally related but functionally divergent series, which show different binding modes corresponding to their agonistic or antagonistic nature. In addition, we present a third progesterone receptor ligand binding domain dimer bound to an agonist in monomer A and an antagonist in monomer B, which display binding modes in agreement with the earlier observation that agonists and antagonists from this series adopt different binding modes. Structural basis for agonism and antagonism for a set of chemically related progesterone receptor modulators.,Lusher SJ, Raaijmakers HC, Vu-Pham D, Dechering K, Lam TW, Brown AR, Hamilton NM, Nimz O, Bosch R, McGuire R, Oubrie A, de Vlieg J J Biol Chem. 2011 Oct 7;286(40):35079-86. Epub 2011 Aug 17. PMID:21849509[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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