Wu3857 at 20:15, 20 August 2019

2019-08-20T20:15:55Z

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CDC37|[https://www.uniprot.org/uniprot/Q16543 Q16543]|Homo sapiens|Cys57, Cys54, Cys64|[http://pfam.xfam.org/fa..."

2019-08-20T20:14:02Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CDC37|[https://www.uniprot.org/uniprot/Q16543 Q16543]|Homo sapiens|Cys57, Cys54, Cys64|[http://pfam.xfam.org/fa..."

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{{#invoke:InfoboxforTarget|run|CDC37|[https://www.uniprot.org/uniprot/Q16543 Q16543]|Homo sapiens|Cys57, Cys54, Cys64|[http://pfam.xfam.org/family/PF03234 CDC37 family]|[[:Category:Hsp90 co-chaperone Cdc37|Ligand list]]|Chaperone}}
==Summary==

===Protein Function ===
Hsp90 co-chaperone Cdc37 is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases, and is upregulated in various cancers. It is thought to play a critical role in directing Hsp90 to its target kinases. The protein–protein complex forms with a KD value of 1.2 mm and is considered to mediate carcinogenesis by stabilizing a variety of different oncogenic kinases in malignant cells. 
CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases. The central domain is the Hsp90chaperone (heat shock protein 90) binding domain. The function of the C-terminal domain is unclear. (From Uniprot, Wikipedia, PMID: 19585625) 

===Cys Function & Property===
From the mutation, homology modeling and other assay, Cys57, Cys54, Cys64 are confirmed to located in/near the celastrol binding pocket. 
[[File:579-function.png|center|600px]]
<div align="center">Possible mechanisms of inactivation of Cdc37 by celastrol</div>
[[File:579-function2.png|center|600px]]
<div align="center">The predicted model of Cdc37_NM complexed with celastrol</div>

* Hydrophobic property:
:[[File:579-hydro.png||600px]]
* SASA:
:Cys57, Cys54, Cys64
: 10.925 A^2 

==Protein Sequence==

MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL 
DRG'''C'''RE'''C'''KRK VAE'''C'''QRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ 
KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT 
FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE 
EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME 
GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES 
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE 
AKEGEEAGPG DPLLEAVPKT GDEKDVSV 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
:Unknown 

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04151 PI3K-Akt signaling pathway] 

==Experimental Evidence==
:Nuclear Magnetic Resonance, Mass Spectrometry

==Reference==
# Sreeramulu S, Gande S L, Göbel M, et al. '''Molecular mechanism of inhibition of the human protein complex Hsp90–Cdc37, a kinome chaperone–cochaperone, by triterpene celastrol[J].''' Angewandte Chemie International Edition, 2009, 48(32): 5853-5855. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19585625 19585625] 
# Duan Y, Jin H, Yu H, et al. '''Computational investigation of interactions between Cdc37 and celastrol[J].''' Molecular Simulation, 2013, 39(4): 270-278. DOI:10.1080/08927022.2012.718439.

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Chaperone]]
[[Category:CDC37 family]]
[[Category:PI3K-Akt signaling pathway]]

@@ Line 19: / Line 19: @@
 :[[File:579-hydro.png||600px]]
 * SASA:
-:Cys57, Cys54, Cys64
+:Unknown<br/>
 ==Protein Sequence==

Hsp90 co-chaperone Cdc37 - Revision history

Wu3857 at 20:15, 20 August 2019

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CDC37|[https://www.uniprot.org/uniprot/Q16543 Q16543]|Homo sapiens|Cys57, Cys54, Cys64|[http://pfam.xfam.org/fa..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CDC37|[https://www.uniprot.org/uniprot/Q16543 Q16543]|Homo sapiens|Cys57, Cys54, Cys64|[http://pfam.xfam.org/fa..."