Structure-guided optimization of small molecule c-Abl activators View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-02

AUTHORS

Xuan Hong, Ping Cao, Yoshiaki Washio, Graham Simpson, Nino Campobasso, Jingsong Yang, Jennifer Borthwick, George Burton, Julien Chabanet, Sophie Bertrand, Helen Evans, Robert J. Young, Junya Qu, Hu Li, Josh Cottom, Paris Ward, Hong Zhang, Thau Ho, Donghui Qin, Siegfried Christensen, Martha S. Head

ABSTRACT

c-Abl kinase is maintained in its normal inactive state in the cell through an assembled, compact conformation. We describe two chemical series that bind to the myristoyl site of the c-Abl kinase domain and stimulate c-Abl activation. We hypothesize that these molecules activate c-Abl either by blocking the C-terminal helix from adopting a bent conformation that is critical for the formation of the autoinhibited conformation or by simply providing no stabilizing interactions to the bent conformation of this helix. Structure-based molecular modeling guided the optimization of binding and activation of c-Abl of these two chemical series and led to the discovery of c-Abl activators with nanomolar potency. The small molecule c-Abl activators reported herein could be used as molecular tools to investigate the biological functions of c-Abl and therapeutic implications of its activation. More... »

PAGES

75-87

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10822-014-9731-5

DOI

http://dx.doi.org/10.1007/s10822-014-9731-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026608010

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24573412


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