3eko: Difference between revisions

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-{{Seed}}
-[[Image:3eko.png|left|200px]]
-<!--
+==Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone==
-The line below this paragraph, containing "STRUCTURE_3eko", creates the "Structure Box" on the page.
+<StructureSection load='3eko' size='340' side='right'caption='[[3eko]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3eko]] is a 2 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=3EKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKO FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PYU:2-(1H-PYRROL-1-YLCARBONYL)BENZENE-1,3,5-TRIOL'>PYU</scene></td></tr>
-{{STRUCTURE_3eko|  PDB=3eko  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eko OCA], [https://pdbe.org/3eko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eko RCSB], [https://www.ebi.ac.uk/pdbsum/3eko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eko 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>
+== 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/ek/3eko_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/main_output.php?pdb_ID=3eko ConSurf].
+<div style="clear:both"></div>
-===Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone===
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_18929486}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 18929486 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_18929486}}
-==About this Structure==
-EKO is a 2 chains structure of sequences 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=3EKO OCA].
-==Reference==
-Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone., Kung PP, Funk L, Meng J, Collins M, Zhou JZ, Johnson MC, Ekker A, Wang J, Mehta P, Yin MJ, Rodgers C, Davies JF 2nd, Bayman E, Smeal T, Maegley KA, Gehring MR, Bioorg Med Chem Lett. 2008 Dec 1;18(23):6273-8. Epub 2008 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18929486 18929486]
 [[Category: Homo sapiens]]
-[[Category: Gajiwala, K S.]]
+[[Category: Large Structures]]
-[[Category: Alternative splicing]]
+[[Category: Gajiwala KS]]
-[[Category: Atp-binding]]
-[[Category: Chaperone]]
-[[Category: Cytoplasm]]
-[[Category: Hsp90 inhibitor]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Stress response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Dec  5 09:58:43 2008''