|PROSITE documentation PDOC50229 [for PROSITE entry PS50229]|
The WH1 (WASP-Homology 1, or Wiskott-Aldrich homology 1) or EVH1 (Ena/VASP homology 1, or Enabled/Vasodilator-stimulated phosphoprotein homology 1) domain is an ~110 amino acids protein-protein interaction module. WH1 proteins occur in eukaryotes from yeast to mammals and play a role in signaling and regulation of the cytoskeleton. The WH1 domain is usually located in the N-terminal part. A CRIB domain (see <PDOC50108>) or a WH2 domain (see <PDOC51082>) can occur C-terminal to the WH1 domain. Most WH1 domains bind proline-rich sequences: the WASP and the Enabled/VASP families bind to LPPPEP and to FPPPP peptides, respectively, while the Homer/Vesl family binds to PPXXF motifs, and less proline-rich peptides could be ligands as well [1,2,3,4,5].
Tertiary structures of the WH1 domains from different proteins show structure similarities with the pleckstrin homology (PH) domain (see <PDOC50003>) and with the WH1-related Ran binding domain (see <PDOC50196>). The WH1 domain comprises two β-sheets (B1-B7) that form a β-sandwich, capped by a C-terminal α-helix (see <PDB:1XOD>). The principal peptide binding activity is formed by a groove between the strands B1, B2, B6 and B7. Proteins which can bind to WH1 domains are e.g. Zyxin, Vinculin, WASP interacting protein (WIP), metabotropic glutamate receptors and the Listeria monocytogenes ActA protein [4,5].
Some proteins known to contain a WH1 domain:
The profile we developed covers the entire WH1 domain.Last update:
March 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Prehoda K.E. Lee D.J. Lim W.A.|
|Title||Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.|
|2||Authors||Zettl M. Way M.|
|Title||The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs.|
|Source||Curr. Biol. 12:1617-1622(2002).|
|Title||An EVH1/WH1 domain as a key actor in TGFbeta signalling.|
|Source||FEBS Lett. 519:178-180(2002).|
|4||Authors||Krause M. Dent E.W. Bear J.E. Loureiro J.J. Gertler F.B.|
|Title||Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration.|
|Source||Annu. Rev. Cell Dev. Biol. 19:541-564(2003).|
|5||Authors||Harmer N.J. Sivak J.M. Amaya E. Blundell T.L.|
|Title||1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family.|
|Source||FEBS Lett. 579:1161-1166(2005).|