4o09: Difference between revisions

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-'''Unreleased structure'''
-The entry 4o09 is ON HOLD
+==Identification of novel HSP90 / isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington s disease==
+<StructureSection load='4o09' size='340' side='right'caption='[[4o09]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4o09]] 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=4O09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O09 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2R6:8-(2-METHYLPROPYL)-6-(3,6,6-TRIMETHYL-4-OXO-4,5,6,7-TETRAHYDRO-1H-INDOL-1-YL)-3,4-DIHYDROISOQUINOLIN-1(2H)-ONE'>2R6</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=4o09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o09 OCA], [https://pdbe.org/4o09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o09 RCSB], [https://www.ebi.ac.uk/pdbsum/4o09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o09 ProSAT]</span></td></tr>
+</table>
+== 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>
-Authors: Zuccola, H. J., Ernst, J. T.
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-Description: Identification of novel HSP90 / isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington s disease
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Ernst JT]]
+[[Category: Zuccola HJ]]