4l90: Difference between revisions

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==Crystal structure of Human Hsp90 with RL3==
==Crystal structure of Human Hsp90 with RL3==
<StructureSection load='4l90' size='340' side='right' caption='[[4l90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4l90' size='340' side='right'caption='[[4l90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l90]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L90 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l90]] 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=4L90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L90 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RL3:[5-(6-BROMO[1,2,4]TRIAZOLO[4,3-A]PYRIDIN-3-YL)-2,4-DIHYDROXYPHENYL](4-METHYLPIPERAZIN-1-YL)METHANONE'>RL3</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l8z|4l8z]], [[4l91|4l91]], [[4l93|4l93]], [[4l94|4l94]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RL3:[5-(6-BROMO[1,2,4]TRIAZOLO[4,3-A]PYRIDIN-3-YL)-2,4-DIHYDROXYPHENYL](4-METHYLPIPERAZIN-1-YL)METHANONE'>RL3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l90 RCSB], [http://www.ebi.ac.uk/pdbsum/4l90 PDBsum]</span></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=4l90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l90 OCA], [https://pdbe.org/4l90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l90 RCSB], [https://www.ebi.ac.uk/pdbsum/4l90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l90 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: He, J]]
[[Category: Homo sapiens]]
[[Category: Li, J]]
[[Category: Large Structures]]
[[Category: Ren, J]]
[[Category: He J]]
[[Category: Xiong, B]]
[[Category: Li J]]
[[Category: Yang, M]]
[[Category: Ren J]]
[[Category: Atp hydrolysis]]
[[Category: Xiong B]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Yang M]]
[[Category: Hsp90n-hsp90n inhibitor complex]]

Latest revision as of 17:33, 8 November 2023

Crystal structure of Human Hsp90 with RL3Crystal structure of Human Hsp90 with RL3

Structural highlights

4l90 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 2.001Å
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

4l90, resolution 2.00Å

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