3eko: Difference between revisions

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[[Image:3eko.png|left|200px]]


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==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=''>
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== 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>
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<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>
===Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone===
== 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]]
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Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/3eko_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_18929486}}
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    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
[[3eko]] is a 2 chain structure of [[Heat Shock Proteins]] 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=3EKO OCA].  
</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>


==See Also==
==See Also==
*[[Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:18929486</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[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]]

Latest revision as of 12:48, 21 February 2024

Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperoneDihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone

Structural highlights

3eko is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
  2. ↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200

3eko, resolution 1.55Å

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