2yej: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='2yej' size='340' side='right'caption='[[2yej]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2yej' size='340' side='right'caption='[[2yej]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2yej]] 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=2YEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XQK:METHYL+5-ISOXAZOL-5-YL-3-METHYL-1H-PYRAZOLE-4-CARBOXYLATE'>XQK</scene>, <scene name='pdbligand=ZZ3:4-METHYL-6-(METHYLSULFANYL)-1,3,5-TRIAZIN-2-AMINE'>ZZ3</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XQK:METHYL+5-ISOXAZOL-5-YL-3-METHYL-1H-PYRAZOLE-4-CARBOXYLATE'>XQK</scene>, <scene name='pdbligand=ZZ3:4-METHYL-6-(METHYLSULFANYL)-1,3,5-TRIAZIN-2-AMINE'>ZZ3</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=2yej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yej OCA], [https://pdbe.org/2yej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yej RCSB], [https://www.ebi.ac.uk/pdbsum/2yej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yej 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=2yej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yej OCA], [https://pdbe.org/2yej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yej RCSB], [https://www.ebi.ac.uk/pdbsum/2yej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yej 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> | |||
==See Also== | ==See Also== | ||
Line 17: | Line 17: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baker | [[Category: Baker LM]] | ||
[[Category: Hubbard | [[Category: Hubbard RE]] | ||
[[Category: Roughley | [[Category: Roughley SD]] | ||
Latest revision as of 13:51, 20 December 2023
HSP90 inhibitors and drugs from fragment and virtual screeningHSP90 inhibitors and drugs from fragment and virtual screening
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
|
|