View source for 3rlq


==Co-crystal structure of the HSP90 ATP binding domain in complex with 4-(2,4-dichloro-5-methoxyphenyl)-2-methyl-7H-pyrrolo[2,3-d]pyrimidine-5- carbonitrile==
<StructureSection load='3rlq' size='340' side='right'caption='[[3rlq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rlq]] 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=3RLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RLQ 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3RQ:4-(2,4-DICHLORO-5-METHOXYPHENYL)-2-METHYL-7H-PYRROLO[2,3-D]PYRIMIDINE-5-CARBONITRILE'>3RQ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3rlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rlq OCA], [https://pdbe.org/3rlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rlq RCSB], [https://www.ebi.ac.uk/pdbsum/3rlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rlq 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: Bergqvist S]]
[[Category: Gajiwala KS]]
[[Category: Hickey MJ]]
[[Category: Huang B]]
[[Category: Kania R]]
[[Category: Kung P-P]]
[[Category: Maegley K]]
[[Category: McClellan G]]
[[Category: Mehta PP]]
[[Category: Richardson P]]
[[Category: Sinnema P-J]]
[[Category: Wang F]]
[[Category: Wang J]]