3ft8: Difference between revisions

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 ==Structure of HSP90 bound with a noval fragment.==
-<StructureSection load='3ft8' size='340' side='right' caption='[[3ft8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3ft8' size='340' side='right'caption='[[3ft8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ft8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FT8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ft8]] 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=3FT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FT8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MOJ:(5E,7S)-2-AMINO-7-(4-FLUORO-2-PYRIDIN-3-YLPHENYL)-4-METHYL-7,8-DIHYDROQUINAZOLIN-5(6H)-ONE+OXIME'>MOJ</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ft5|3ft5]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MOJ:(5E,7S)-2-AMINO-7-(4-FLUORO-2-PYRIDIN-3-YLPHENYL)-4-METHYL-7,8-DIHYDROQUINAZOLIN-5(6H)-ONE+OXIME'>MOJ</scene></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 Homo sapiens])</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=3ft8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ft8 OCA], [https://pdbe.org/3ft8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ft8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ft8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ft8 ProSAT]</span></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=3ft8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ft8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ft8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ft8 PDBsum]</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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ft8_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ft8_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=3ft8 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Heat shock protein 90 (Hsp90) plays a key role in stress response and protection of the cell against the effects of mutation. Herein we report the identification of an Hsp90 inhibitor identified by fragment screening using a high-concentration biochemical assay, as well as its optimisation by in silico searching coupled with a structure-based drug design (SBDD) approach.
-Fragment-based identification of Hsp90 inhibitors.,Barker JJ, Barker O, Boggio R, Chauhan V, Cheng RK, Corden V, Courtney SM, Edwards N, Falque VM, Fusar F, Gardiner M, Hamelin EM, Hesterkamp T, Ichihara O, Jones RS, Mather O, Mercurio C, Minucci S, Montalbetti CA, Muller A, Patel D, Phillips BG, Varasi M, Whittaker M, Winkler D, Yarnold CJ ChemMedChem. 2009 Jun;4(6):963-6. PMID:19301319<ref>PMID:19301319</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Heat Shock Proteins|Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
@@ Line 36: / Line 28: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Barker, J B]]
+[[Category: Large Structures]]
-[[Category: Cheng, R K.Y]]
+[[Category: Barker JB]]
-[[Category: Felicetti, B]]
+[[Category: Cheng RKY]]
-[[Category: Palan, S]]
+[[Category: Felicetti B]]
-[[Category: Atp-binding]]
+[[Category: Palan S]]
-[[Category: Chaperone]]
-[[Category: Hsp90 n-terminal nucleotide binding domain]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Stress response]]