5cf0: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5cf0]] 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=5CF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CF0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5cf0]] 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=5CF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CF0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FJS:N-{3-[2,4-DIHYDROXY-5-(ISOQUINOLIN-4-YL)PHENYL]-4-(4-METHOXYPHENYL)-1,2-OXAZOL-5-YL}CYCLOPROPANECARBOXAMIDE'>FJS</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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FJS:N-{3-[2,4-DIHYDROXY-5-(ISOQUINOLIN-4-YL)PHENYL]-4-(4-METHOXYPHENYL)-1,2-OXAZOL-5-YL}CYCLOPROPANECARBOXAMIDE'>FJS</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=5cf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cf0 OCA], [https://pdbe.org/5cf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cf0 RCSB], [https://www.ebi.ac.uk/pdbsum/5cf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cf0 ProSAT]</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=5cf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cf0 OCA], [https://pdbe.org/5cf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cf0 RCSB], [https://www.ebi.ac.uk/pdbsum/5cf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cf0 ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 19:08, 8 November 2023

Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ6Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ6

Structural highlights

5cf0 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 1.8Å
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

5cf0, resolution 1.80Å

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