3b27: Difference between revisions

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[[Image:3b27.jpg|left|200px]]


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==Hsp90 alpha N-terminal domain in complex with an inhibitor Ro4919127==
The line below this paragraph, containing "STRUCTURE_3b27", creates the "Structure Box" on the page.
<StructureSection load='3b27' size='340' side='right'caption='[[3b27]], [[Resolution|resolution]] 1.50&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'>[[3b27]] 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=3B27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B27 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#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=B2T:4-(2-CHLOROPHENYL)-6-(METHYLSULFANYL)-1,3,5-TRIAZIN-2-AMINE'>B2T</scene></td></tr>
{{STRUCTURE_3b27|  PDB=3b27  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b27 OCA], [https://pdbe.org/3b27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b27 RCSB], [https://www.ebi.ac.uk/pdbsum/3b27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b27 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 alpha N-terminal domain in complex with an inhibitor Ro4919127===
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
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{{ABSTRACT_PUBMED_21875802}}
 
==About this Structure==
[[3b27]] 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=3B27 OCA].
 
==Reference==
<ref group="xtra">PMID:021875802</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Fukami, T A.]]
[[Category: Large Structures]]
[[Category: Ono, N.]]
[[Category: Fukami TA]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Ono N]]

Latest revision as of 17:03, 13 March 2024

Hsp90 alpha N-terminal domain in complex with an inhibitor Ro4919127Hsp90 alpha N-terminal domain in complex with an inhibitor Ro4919127

Structural highlights

3b27 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 1.5Å
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

3b27, resolution 1.50Å

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