Abstract：
:Receptor tyrosine kinases (RTKs) are key regulators of normal cellular processes and have a critical role in the development and progression of many diseases. RTK ligand-induced stimulation leads to activation of the cytoplasmic kinase domain that controls the intracellular signalling. Although the kinase domain of RTKs has been extensively studied using X-ray analysis, the kinase insert domain (KID) and the C-terminal are partially or fully missing in all reported structures. We communicate the first structural model of the full-length RTK KIT cytoplasmic domain, a crucial target for cancer therapy. This model was achieved by integration of ab initio KID and C-terminal probe models into an X-ray structure, and by their further exploration through molecular dynamics (MD) simulation. An extended (2-µs) MD simulation of the proper model provided insight into the structure and conformational dynamics of the full-length cytoplasmic domain of KIT, which can be exploited in the description of the KIT transduction processes.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Inizan F,Hanna M,Stolyarchuk M,Chauvot de Beauchêne I,Tchertanov Ldoi
10.1038/s41598-020-62460-7subject
Has Abstractpub_date
2020-03-25 00:00:00pages
5401issue
1issn
2045-2322pii
10.1038/s41598-020-62460-7journal_volume
10pub_type
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