4xir: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xir]] 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=4XIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xir]] 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=4XIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40X:(6S)-2-CHLORO-8,11,11-TRIMETHYL-9-OXO-6-PROPYL-6,7,9,10,11,12-HEXAHYDROINDOLO[2,1-D][1,5]BENZOXAZEPINE-3-CARBOXAMIDE'>40X</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40X:(6S)-2-CHLORO-8,11,11-TRIMETHYL-9-OXO-6-PROPYL-6,7,9,10,11,12-HEXAHYDROINDOLO[2,1-D][1,5]BENZOXAZEPINE-3-CARBOXAMIDE'>40X</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xir OCA], [https://pdbe.org/4xir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xir RCSB], [https://www.ebi.ac.uk/pdbsum/4xir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xir 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=4xir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xir OCA], [https://pdbe.org/4xir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xir RCSB], [https://www.ebi.ac.uk/pdbsum/4xir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xir ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | [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== |
Latest revision as of 16:01, 1 March 2024
Discovery of novel oxazepine and diazepine carboxamides as two new classes of heat shock protein 90 inhibitorsDiscovery of novel oxazepine and diazepine carboxamides as two new classes of heat shock protein 90 inhibitors
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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