For example, in the AU-rich element RNA-binding protein KSRP, which has 4 KH domains, KH domains 3 and 4 behave as independent binding modules to interact with different regions of the AU-rich RNA targets.

[2][3] Autoantibodies to NOVA1, a KH domain protein, cause paraneoplastic opsoclonus ataxia.

[4] KH domains bind to either RNA or single stranded DNA.

[5] The binding cleft is hydrophobic in nature with a variety of additional protein specific interactions to stabilise the complex.

While both types share a minimal consensus sequence motif they have different structural folds.