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These 3D structure changes affect both the extracellular and intracellular parts (domains) of the receptor.
Mutations in the intracellular part of this receptor are also associated with certain types of leukemia.
The c-kit molecule comprises a long extracellular domain, a transmembrane segment, and an intracellular part.
The soluble intracellular parts of the protein are highly charged, containing 31 positively charged and 53 negatively charged residues.
The extracellular region of the receptor consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain.
Mutations generally occur in the DNA encoding the intracellular part (exon 11), which acts as a tyrosine kinase to activate other enzymes.
It docks to the intracellular part of the Reelin very low density lipoprotein receptor (VLDLR) and apoE receptor type 2 (ApoER2) and becomes tyrosine-phosphorylated following binding of Reelin to cortical neurons.