3tuh: Difference between revisions
New page: '''Unreleased structure''' The entry 3tuh is ON HOLD Authors: YING, W Description: Crystal Structure of the N-terminal domain of an HSP90 in the presence of an the inhibitor ganetespib |
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==Crystal Structure of the N-terminal domain of an HSP90 in the presence of an the inhibitor ganetespib== | |||
<StructureSection load='3tuh' size='340' side='right'caption='[[3tuh]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tuh]] is a 2 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=3TUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUH 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TUH:5-[2,4-DIHYDROXY-5-(PROPAN-2-YL)PHENYL]-4-(1-METHYL-1H-INDOL-5-YL)-2,4-DIHYDRO-3H-1,2,4-TRIAZOL-3-ONE'>TUH</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=3tuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuh OCA], [https://pdbe.org/3tuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuh RCSB], [https://www.ebi.ac.uk/pdbsum/3tuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuh 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 == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Ying W]] | |||