EVH1 domain
| EVH1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
structure of the n-wasp evh1 domain-wip complex
|
|||||||||
| Identifiers | |||||||||
| Symbol | EVH1 | ||||||||
| Pfam | PF00568 | ||||||||
| Pfam clan | CL0266 | ||||||||
| InterPro | IPR000697 | ||||||||
| SMART | WH1 | ||||||||
| SCOP | 1evh | ||||||||
| SUPERFAMILY | 1evh | ||||||||
| CDD | cd00837 | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
The EVH1 domain (also known as the WH1, RanBP1-WASP, or enabled/VASP homology 1 domain) is an evolutionary conserved protein domain.
The EVH1 domain is found in multi-domain Ena/Vasp homology proteins implicated in a diverse range of signalling, nuclear transport and cytoskeletal events. This domain of around 115 amino acids is present in species ranging from yeast to mammals. Many EVH1-containing proteins associate with actin-based structures and play a role in cytoskeletal organisation. EVH1 domains recognise and bind the proline-rich motif FPPPP with low-affinity, further interactions then form between flanking residues.
WASP family proteins contain an EVH1 (WH1) in their N-terminus which bind proline-rich sequences in the WASP interacting protein. Proteins of the RanBP1 family contain a WH1 domain in their N-terminal region, which seems to bind a different sequence motif present in the C-terminal part of RanGTP protein.
Tertiary structure of the WH1 domain of the Mena protein revealed structure similarities with the pleckstrin (PH) domain. The overall fold consists of a compact parallel beta-sandwich, closed along one edge by a long alpha helix. A highly conserved cluster of three surface-exposed aromatic side-chains forms the recognition site for the molecule's target ligands.
...
Wikipedia