View source for 3nmq


==Hsp90b N-terminal domain in complex with EC44, a pyrrolo-pyrimidine methoxypyridine inhibitor==
<StructureSection load='3nmq' size='340' side='right'caption='[[3nmq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nmq]] 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=3NMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NMQ 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7PP:5-{2-AMINO-4-CHLORO-7-[(4-METHOXY-3,5-DIMETHYLPYRIDIN-2-YL)METHYL]-7H-PYRROLO[2,3-D]PYRIMIDIN-5-YL}-2-METHYLPENT-4-YN-2-OL'>7PP</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=3nmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmq OCA], [https://pdbe.org/3nmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nmq RCSB], [https://www.ebi.ac.uk/pdbsum/3nmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nmq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HS90B_HUMAN HS90B_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:16478993</ref> <ref>PMID:19696785</ref> 

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arndt JW]]
[[Category: Giza K]]
[[Category: Harning EK]]
[[Category: Kehry MR]]
[[Category: Li P]]
[[Category: Luchetti D]]
[[Category: Manning A]]
[[Category: Rabah D]]
[[Category: Shi J]]
[[Category: Yun TJ]]