5xrb: Difference between revisions
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==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5== | |||
<StructureSection load='5xrb' size='340' side='right'caption='[[5xrb]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5xrb]] 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=5XRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8DU:N-[3-[5-chloranyl-2,4-bis(oxidanyl)phenyl]-4-(4-methoxyphenyl)-1,2-oxazol-5-yl]cyclopropanecarboxamide'>8DU</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=5xrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrb OCA], [https://pdbe.org/5xrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrb RCSB], [https://www.ebi.ac.uk/pdbsum/5xrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrb 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> | |||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: He | __TOC__ | ||
[[Category: Li | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: He JH]] | |||
[[Category: Li J]] | |||
[[Category: Shi F]] | |||
[[Category: Xiong B]] | |||
Latest revision as of 13:19, 27 March 2024
Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ5
Structural highlights
FunctionHS90A_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 AlsoReferences
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