2w0g: Difference between revisions
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<StructureSection load='2w0g' size='340' side='right'caption='[[2w0g]], [[Resolution|resolution]] 1.88Å' scene=''> | <StructureSection load='2w0g' size='340' side='right'caption='[[2w0g]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2w0g]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2w0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0G FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us7|1us7]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1us7|1us7]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0g OCA], [https://pdbe.org/2w0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0g RCSB], [https://www.ebi.ac.uk/pdbsum/2w0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CDC37_HUMAN CDC37_HUMAN]] Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.<ref>PMID:8666233</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:51, 7 July 2021
HSP90 CO-CHAPERONE CDC37HSP90 CO-CHAPERONE CDC37
Structural highlights
Function[CDC37_HUMAN] Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases. The catalytic domains of these kinases are stabilized by Cdc37, and their proper folding and functioning is dependent on Hsp90. Here, we present the x-ray crystal structure of the 16-kDa middle domain of human Cdc37 at 1.88 angstroms resolution and the structure of this domain in complex with the 23-kDa N-terminal domain of human Hsp90 based on heteronuclear solution state NMR data and docking. Our results demonstrate that the middle domain of Cdc37 exists as a monomer. NMR and mutagenesis experiments reveal Leu-205 in Cdc37 as a key residue enabling complex formation. These findings can be very useful in the development of small molecule inhibitors against cancer. The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy.,Sreeramulu S, Jonker HR, Langer T, Richter C, Lancaster CR, Schwalbe H J Biol Chem. 2009 Feb 6;284(6):3885-96. Epub 2008 Dec 10. PMID:19073599[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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