3b25: Difference between revisions

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[[Image:3b25.png|left|200px]]


{{STRUCTURE_3b25|  PDB=3b25  |  SCENE=  }}
==Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194==
 
<StructureSection load='3b25' size='340' side='right'caption='[[3b25]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
===Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3b25]] 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=3B25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B25 FirstGlance]. <br>
{{ABSTRACT_PUBMED_21875802}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2K:4-METHYL-6-(TOLUENE-4-SULFONYL)-PYRIMIDIN-2-YLAMINE'>B2K</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b25 OCA], [https://pdbe.org/3b25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b25 RCSB], [https://www.ebi.ac.uk/pdbsum/3b25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b25 ProSAT]</span></td></tr>
[[3b25]] 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=3B25 OCA].  
</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>


==See Also==
==See Also==
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021875802</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[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 CH4675194Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194

Structural highlights

3b25 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 1.75Å
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

3b25, resolution 1.75Å

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