3bm9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BM9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3bm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BM9 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BXZ:4-BROMO-6-(6-HYDROXY-1,2-BENZISOXAZOL-3-YL)BENZENE-1,3-DIOL'>BXZ</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bm9 OCA], [https://pdbe.org/3bm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bm9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bm9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bm9 OCA], [https://pdbe.org/3bm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bm9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bm9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bm9 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bm9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Heat shock protein 90 (Hsp90) is a molecular chaperone that is responsible for activating many signaling proteins and is a promising target in tumor biology. We have identified small-molecule benzisoxazole derivatives as Hsp90 inhibitors. Crystallographic studies show that these compounds bind in the ATP binding pocket interacting with the Asp93. Structure based optimization led to the identification of potent analogues, such as 13, with good biochemical profiles. | ||
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| - | Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90.,Gopalsamy A, Shi M, Golas J, Vogan E, Jacob J, Johnson M, Lee F, Nilakantan R, Petersen R, Svenson K, Chopra R, Tam MS, Wen Y, Ellingboe J, Arndt K, Boschelli F J Med Chem. 2008 Feb 14;51(3):373-5. Epub 2008 Jan 16. PMID:18197612<ref>PMID:18197612</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3bm9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arndt | + | [[Category: Arndt K]] |
| - | [[Category: Boschelli | + | [[Category: Boschelli F]] |
| - | [[Category: Chopra | + | [[Category: Chopra R]] |
| - | [[Category: Ellingboe | + | [[Category: Ellingboe J]] |
| - | [[Category: Golas | + | [[Category: Golas J]] |
| - | [[Category: Gopalsamy | + | [[Category: Gopalsamy A]] |
| - | [[Category: Jacob | + | [[Category: Jacob J]] |
| - | [[Category: Johnson | + | [[Category: Johnson J]] |
| - | [[Category: Lee | + | [[Category: Lee F]] |
| - | [[Category: Nilakantan | + | [[Category: Nilakantan R]] |
| - | [[Category: Peterson | + | [[Category: Peterson R]] |
| - | [[Category: Shi | + | [[Category: Shi M]] |
| - | [[Category: Svenson | + | [[Category: Svenson K]] |
| - | [[Category: Tam | + | [[Category: Tam MS]] |
| - | [[Category: Vogan | + | [[Category: Vogan EM]] |
| - | [[Category: Wen | + | [[Category: Wen Y]] |
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Current revision
Discovery of Benzisoxazoles as Potent Inhibitors of Chaperone Hsp90
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Categories: Homo sapiens | Large Structures | Arndt K | Boschelli F | Chopra R | Ellingboe J | Golas J | Gopalsamy A | Jacob J | Johnson J | Lee F | Nilakantan R | Peterson R | Shi M | Svenson K | Tam MS | Vogan EM | Wen Y
