4o05: Difference between revisions

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 ==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='4o05' size='340' side='right' caption='[[4o05]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+<StructureSection load='4o05' size='340' side='right'caption='[[4o05]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4o05]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O05 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4o05]] 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=4O05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O05 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2Q9:2,7,7-TRIMETHYL-9-[1-OXO-8-(PROPAN-2-YLAMINO)-1,2,3,4-TETRAHYDROISOQUINOLIN-6-YL]-1,2,3,4,6,7,8,9-OCTAHYDRO-5H-BETA-CARBOLIN-5-ONE'>2Q9</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2Q9:2,7,7-TRIMETHYL-9-[1-OXO-8-(PROPAN-2-YLAMINO)-1,2,3,4-TETRAHYDROISOQUINOLIN-6-YL]-1,2,3,4,6,7,8,9-OCTAHYDRO-5H-BETA-CARBOLIN-5-ONE'>2Q9</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o04|4o04]], [[4o06|4o06]], [[4o09|4o09]], [[4o0b|4o0b]]</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=4o05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o05 OCA], [https://pdbe.org/4o05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o05 RCSB], [https://www.ebi.ac.uk/pdbsum/4o05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o05 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o05 OCA], [http://pdbe.org/4o05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o05 RCSB], [http://www.ebi.ac.uk/pdbsum/4o05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o05 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 4o05" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Ernst, J T]]
+[[Category: Large Structures]]
-[[Category: Zuccola, H J]]
+[[Category: Ernst JT]]
-[[Category: Chaperone]]
+[[Category: Zuccola HJ]]
-[[Category: Chaperone-chaperone inhibitor complex]]