Final answer:
The binding of an antibody to the extracellular domain of receptor tyrosine kinases (RTKs) would likely activate the kinase, since RTK activation is generally achieved through dimerization and subsequent autophosphorylation.
Step-by-step explanation:
If cells containing the receptor tyrosine kinases (RTKs) were exposed to an antibody that is specific for the extracellular domain of an RTK, and this antibody binds to the RTK bringing together two RTK molecules, it would likely lead to the activation of the kinase. This is because RTKs are typically activated through a process of dimerization , which involves two RTKs coming together. When signaling molecules bind to the extracellular domains, the RTKs dimerize and the tyrosine residues on the intracellular domain are autophosphorylation. , triggering a cellular response. As described in the reference material, the dimerization is an essential first step leading to autophosphorylation of tyrosine residues, which then sets off a cascade that ultimately produces a cellular response. Since the binding of antibodies to RTKs mimics the natural dimerization process, the introduction of the specific antibody would be expected to activate the kinase.