4egi: Difference between revisions
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==Hsp90-alpha ATPase domain in complex with 2-Amino-4-ethylthio-6-methyl-1,3,5-triazine== | ==Hsp90-alpha ATPase domain in complex with 2-Amino-4-ethylthio-6-methyl-1,3,5-triazine== | ||
<StructureSection load='4egi' size='340' side='right' caption='[[4egi]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='4egi' size='340' side='right'caption='[[4egi]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4egi]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4egi]] 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=4EGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EGI FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2J:4-(ETHYLSULFANYL)-6-METHYL-1,3,5-TRIAZIN-2-AMINE'>B2J</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2J:4-(ETHYLSULFANYL)-6-METHYL-1,3,5-TRIAZIN-2-AMINE'>B2J</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=4egi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egi OCA], [https://pdbe.org/4egi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4egi RCSB], [https://www.ebi.ac.uk/pdbsum/4egi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4egi ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Heat Shock | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chen WJ]] | ||
[[Category: | [[Category: Wood SP]] | ||
Revision as of 10:10, 28 September 2022
Hsp90-alpha ATPase domain in complex with 2-Amino-4-ethylthio-6-methyl-1,3,5-triazineHsp90-alpha ATPase domain in complex with 2-Amino-4-ethylthio-6-methyl-1,3,5-triazine
Structural highlights
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] Publication Abstract from PubMedCEfrag is a new fragment screening technology based on affinity capillary electrophoresis (ACE). Here we report on the development of a mobility shift competition assay using full-length human heat shock protein 90alpha (Hsp90alpha), radicicol as the competitor probe ligand, and successful screening of the Selcia fragment library. The CEfrag assay was able to detect weaker affinity (IC(50) >500 microM) fragments than were detected by a fluorescence polarization competition assay using FITC-labeled geldanamycin. The binding site of selected fragments was determined by co-crystallization with recombinant Hsp90alpha N-terminal domain and X-ray analysis. The results of this study confirm that CEfrag is a sensitive microscale technique enabling detection of fragments binding to the biological target in near-physiological solution. Fragment Screening Using Capillary Electrophoresis (CEfrag) for Hit Identification of Heat Shock Protein 90 ATPase Inhibitors.,Austin C, Pettit SN, Magnolo SK, Sanvoisin J, Chen W, Wood SP, Freeman LD, Pengelly RJ, Hughes DE J Biomol Screen. 2012 May 9. PMID:22573733[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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