WH1 domain

A highly conserved cluster of three surface-exposed aromatic side-chains forms the recognition site for the molecule's target ligands.

WASP is defective in Wiskott–Aldrich syndrome (WAS) whereby in most patient cases, the majority of point mutations occur within the N-terminal WH1 domain.

A highly conserved cluster of three surface-exposed aromatic side-chains forms the recognition site for the molecules target ligands.

EVH1 domains recognise and bind the proline-rich motif FPPPP with low-affinity, further interactions then form between flanking residues.

[5][8] The EVH1 domain is found in multi-domain Ena/Vasp homology proteins implicated in a diverse range of signalling, nuclear transport and cytoskeletal events.