Abstract
c-Src kinase is a non-receptor tyrosine kinase that aberrantly phosphorylates several signaling proteins in different cancers. It is a multidomain protein comprising N-terminal disordered SH4 and globular SH3, SH2, and kinase (SH1) domains. The regulatory domain SH3 has been shown to form an intramolecular fuzzy complex with the disordered SH4 domain during c-Src activity and upregulation. However, studying the conformations of individual domains, especially disordered regions, during such interactions remains a technical challenge.
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