This page provides information on WW domains.
Please forward suggestions/comments/correction to
Peer Bork or Marius Sudol
Peer.Bork@embl.org or sudol@rockvax.rockefeller.edu
Short progress headlines
- The 3D structure of YAP WW with and without bound peptide has been solved by NMR.
- Various WW domains have been expressed and ligand-binding studies are under way.
- The major binding theme appears to be a proline dipeptide followed by an aromate (e.g. (AP)PP(AP)Y in YAP).
- WW domains have been shown to compete with SH3 domains for several substrates.
- WW-ligand interaction appears to be criticla in several diseases including muscular dystrophy and Liddle's syndrome.
- The characterisation of several proteins containing WW is progressing (e.g. RSP5, a ubiquitin ligase or the bAPP-binding protein FE65).
- creation date: December 15, 1994
- last sequence update: April 15, 1996
- last modification: April 20, 1996
Last modified April 30, 1996