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Molecular Biology of the Cell. 4th edition.

Studying Gene Expression and Function

Dominant-negative effects occur when cells express mutant proteins that impair the activity of the cells' endogenous functional counterpart. This usually involves a mutation in a site required for the protein's function, but not required for binding other proteins.

For example, FGFR activation involves two FGFR molecules dimerising via a dimerising region, and then autophosphorylating via a kinase domain. A dominant-negative variant could be an FGFR with a mutation in (or a deletion of) the kinase active site, so this variant is able to dimerise with another FGFR but then fails to activate. Whenever this mutant dimerises with a "healthy" variant, the binding partner is unable to do its job, which overall reduces the amount of functional FGFR. The effect of expressing this mutant variant is dominant (it manifests even when a wildtype allele is present), and negative (it generates a loss of function).

This was done here: Article Expression of a Dominant Negative FGF Receptor Inhibits Axon...

To design a new dominant-negative variant, you need detailed knowledge of how the wildtype protein functions.

The closest example to this concept is competitive inhibition, where the inhibitor and the original reactant compete at the same binding site. Likewise, in dominant negative effect, the mutant protein compete with the wild type protein at the same target binding site. So the mutant protein could bind to the target but remains unable to exert its function (if the mutation is in functional domains for example).

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