2yi5: Difference between revisions

New page: '''Unreleased structure''' The entry 2yi5 is ON HOLD Authors: Roe, S.M., Prodromou, C., Pearl, L.H. Description: Structural characterization of 5-Aryl-4-(5-substituted-2-4-dihydroxyphe...
 
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'''Unreleased structure'''


The entry 2yi5 is ON HOLD
==Structural characterization of 5-Aryl-4-(5-substituted-2-4- dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors.==
<StructureSection load='2yi5' size='340' side='right'caption='[[2yi5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yi5]] 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=2YI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YI5 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YI5:4-CHLORO-6-[5-(3,4-DIMETHOXYPHENYL)-1,2,3-THIADIAZOL-4-YL]BENZENE-1,3-DIOL'>YI5</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=2yi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yi5 OCA], [https://pdbe.org/2yi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yi5 RCSB], [https://www.ebi.ac.uk/pdbsum/2yi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yi5 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: Roe, S.M., Prodromou, C., Pearl, L.H.
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
Description: Structural characterization of 5-Aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors.
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Pearl LH]]
[[Category: Prodromou C]]
[[Category: Roe SM]]

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