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3bm9
From Proteopedia
(Difference between revisions)
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==Discovery of Benzisoxazoles as Potent Inhibitors of Chaperone Hsp90== | ==Discovery of Benzisoxazoles as Potent Inhibitors of Chaperone Hsp90== | ||
| - | <StructureSection load='3bm9' size='340' side='right' caption='[[3bm9]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3bm9' size='340' side='right'caption='[[3bm9]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bm9]] is a 1 chain structure with sequence from [ | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BXZ:4-BROMO-6-(6-HYDROXY-1,2-BENZISOXAZOL-3-YL)BENZENE-1,3-DIOL'>BXZ</scene></td></tr> | + | </td></tr><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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bmy|3bmy]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bmy|3bmy]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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]] | ||
| Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
| - | *[[Heat Shock | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Arndt, K]] | [[Category: Arndt, K]] | ||
[[Category: Boschelli, F]] | [[Category: Boschelli, F]] | ||
Revision as of 08:19, 19 January 2022
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, M S | Vogan, E M | Wen, Y | Alternative splicing | Atp binding domain | Atp-binding | Chaperone | Cytoplasm | Nucleotide-binding | Phosphoprotein | Stress response

