Drug design is an important part of the job description of a medicinal chemist. In order to design a drug that serves as the antagonist to a novel tyrosine kinase receptor, it is important to understand the properties of the receptor itself, and design molecules based on how those properties can be counteracted.
The first approach to be taken in order to establish a lead compound would be to search for a biomolecule that strongly binds to the N-terminus binding region of the receptor. In order to be an effective inhibitor, the lead compound should bind the receptor with a stronger affinity that the native ligand of the receptor.
Hence, it is important to ascertain the properties and mechanism of action of the novel kinase receptor, and conduct comparative binding assays between the receptor and native ligand, and the receptor and test biomolecule.
The second approach to be taken is to ensure the lead compound functions as a receptor antagonist, not an agonist. This means that the biomolecule must inhibit the enzymatic activity of the receptor upon binding to it.
Hence, biochemical assays designed to measure the kinetics of the receptor activity need to be conducted, with a positive control of receptor bound to its native ligand, the negative control of an unbound receptor, and the test molecule bound to the receptor. If the biomolecule being tested functions as an antagonist, its kinetics should match up with those of the negative control.