2ye2: Difference between revisions

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[[Image:2ye2.jpg|left|200px]]


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==HSP90 inhibitors and drugs from fragment and virtual screening==
The line below this paragraph, containing "STRUCTURE_2ye2", creates the "Structure Box" on the page.
<StructureSection load='2ye2' size='340' side='right'caption='[[2ye2]], [[Resolution|resolution]] 1.90&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'>[[2ye2]] 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=2YE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YE2 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]] 1.9&#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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XQI:METHYL+2-(3,5-DIHYDROXYPHENYL)ETHANOATE'>XQI</scene></td></tr>
{{STRUCTURE_2ye2|  PDB=2ye2  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ye2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ye2 OCA], [https://pdbe.org/2ye2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ye2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ye2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ye2 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>  


===HSP90 INHIBITORS AND DRUGS FROM FRAGMENT AND VIRTUAL SCREENING===
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
==About this Structure==
<references/>
[[2ye2]] 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=2YE2 OCA].
__TOC__
 
</StructureSection>
==Reference==
<ref group="xtra">PMID:021561141</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Baker, L M.]]
[[Category: Large Structures]]
[[Category: Hubbard, R E.]]
[[Category: Baker LM]]
[[Category: Roughley, S D.]]
[[Category: Hubbard RE]]
[[Category: Atp-binding]]
[[Category: Roughley SD]]
[[Category: Atpase]]
[[Category: Chaperone]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Phosphorylation]]
[[Category: Pu3]]
[[Category: Stress response]]

Latest revision as of 13:50, 20 December 2023

HSP90 inhibitors and drugs from fragment and virtual screeningHSP90 inhibitors and drugs from fragment and virtual screening

Structural highlights

2ye2 is a 1 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 1.9Å
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]

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

2ye2, resolution 1.90Å

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