4nh9
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nh9]] 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=4NH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NH9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nh9]] 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=4NH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NH9 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2LC:2-FLUORO-6-[(3S)-TETRAHYDROFURAN-3-YLAMINO]-4-(3,6,6-TRIMETHYL-4-OXO-4,5,6,7-TETRAHYDRO-1H-INDOL-1-YL)BENZAMIDE'>2LC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2LC:2-FLUORO-6-[(3S)-TETRAHYDROFURAN-3-YLAMINO]-4-(3,6,6-TRIMETHYL-4-OXO-4,5,6,7-TETRAHYDRO-1H-INDOL-1-YL)BENZAMIDE'>2LC</scene></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=4nh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh9 OCA], [https://pdbe.org/4nh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4nh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh9 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=4nh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nh9 OCA], [https://pdbe.org/4nh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4nh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nh9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ENPL_HUMAN ENPL_HUMAN] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.<ref>PMID:18264092</ref> | [https://www.uniprot.org/uniprot/ENPL_HUMAN ENPL_HUMAN] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.<ref>PMID:18264092</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | HSP90 continues to be a target of interest for neurodegeneration indications. Selective knockdown of the HSP90 cytosolic isoforms alpha and beta is sufficient to reduce mutant huntingtin protein levels in vitro. Chemotype-dependent binding conformations of HSP90alpha/beta appear to strongly influence isoform selectivity. The rational design of HSP90alpha/beta inhibitors selective versus the mitochondrial (TRAP1) and endoplasmic reticulum (GRP94) isoforms offers a potential mitigating strategy for mechanism-based toxicities. Better tolerated HSP90 inhibitors would be attractive for targeting chronic neurodegenerative diseases such as Huntington's disease. | ||
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| - | Correlation between chemotype-dependent binding conformations of HSP90alpha/beta and isoform selectivity-Implications for the structure-based design of HSP90alpha/beta selective inhibitors for treating neurodegenerative diseases.,Ernst JT, Liu M, Zuccola H, Neubert T, Beaumont K, Turnbull A, Kallel A, Vought B, Stamos D Bioorg Med Chem Lett. 2014 Jan 1;24(1):204-8. doi: 10.1016/j.bmcl.2013.11.036., Epub 2013 Nov 23. PMID:24332488<ref>PMID:24332488</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4nh9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity
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