One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues.

The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues.

[5] The best-known example is the ribonuclease inhibitor, but other proteins such as the tropomyosin regulator tropomodulin and the toll-like receptor also share the motif.

In fact, the toll-like receptor possesses 10 successive LRR motifs which serve to bind pathogen- and danger-associated molecular patterns.

[7][8][9] An iron sulphur cluster is found at the N-terminus of some proteins containing the leucine-rich repeat variant domain (LRV).