Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins
نویسندگان
چکیده
منابع مشابه
Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.
Hsp90 is an ATP-dependent molecular chaperone, which facilitates the activation and stabilization of hundreds of client proteins in cooperation with a defined set of cofactors. Many client proteins are protein kinases, which are activated and stabilized by Hsp90 in cooperation with the kinase-specific co-chaperone Cdc37. Other Hsp90 co-chaperones, like the ATPase activator Aha1, also are implic...
متن کاملStructure of an Hsp90-Cdc37-Cdk4 complex.
Activation of many protein kinases depends on their interaction with the Hsp90 molecular chaperone system. Recruitment of protein kinase clients to the Hsp90 chaperone system is mediated by the cochaperone adaptor protein Cdc37, which acts as a scaffold, simultaneously binding protein kinases and Hsp90. We have now expressed and purified an Hsp90-Cdc37-Cdk4 complex, defined its stoichiometry, a...
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برهمکنش dnaتیموس گاوی طبیعی (ct-dna) با اتیلن دی آمین تترااستات (edta)در بافرtris-hcl با 8/7 ph ( دراین ph،edta به نمک دی سدیم تبدیل می شود) وسسامول در بافر tris-hcl با4/7 ph مورد بررسی قرار گرفته است. edta و سسامول استفاده فراوانی در تکنولوژی غذایی و صنعت شیمیایی دارند. مدل اتصال dna مربوط بهedta بوسیله اسپکتروفتومتری جذب، دورنگ نمایی حلقوی(cd)، ویسکومتری وژل الکتروفورز بررسی شده است. طیفuv ...
15 صفحه اولMutations Y493G and K546D in human HSP90 disrupt binding of celastrol and reduce interaction with Cdc37
Celastrol, a natural compound derived from the Chinese herb Tripterygium wilfordii Hook F, has been proven to inhibit heat shock protein 90 (HSP90) activity and has attracted much attention because of its promising effects in cancer treatment and in ameliorating degenerative neuron diseases. However, the HSP90 structure involved in celastrol interaction is not known. Here, we report a novel cel...
متن کاملIdentification of the Factors Responsible for the Interaction of Hsp90 and its Client Proteins
Hsp90 is a stress protein that acts as a molecular chaperone and is known to assist in the maturation, folding and stabilization of various cellular proteins known as ‘client proteins’. However, the factors that drive the interaction between Hsp90 and its client proteins are not well understood. In the present investigation, we predicted the basis of the different interaction of Hsp90 with both...
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ژورنال
عنوان ژورنال: Oncogene
سال: 2013
ISSN: 0950-9232,1476-5594
DOI: 10.1038/onc.2013.519