GEL Domain
GEL domain from human plasma gelsolin, with bound calcium ions in red.
Domain Binding and Function
Also know as the gelsolin/severin/villin homology domain, the gelsolin homology domain (GEL) is a 120–150 amino acid domain found in a variety of proteins involved in cytoskeletal regulation, particularly in proteins that function in actin severing. The GEL domain has both calcium binding and actin binding activity, such that actin binding is calcium regulated. The gelsolin protein, composed of six GEL domains, binds to the barbed ends of actin filaments preventing monomer exchange and acting as an end-blocking or capping protein for the actin filament. In addition, gelsolin can promote actin nucleation to create new filaments and sever existing filaments.
Structure Reference
- Robinson, R.C. et al. (1999) Science 286(5446), 1939-1942.
Examples of Domain Proteins
Binding Examples
| GEL Domain Proteins | Binding Partners |
|---|---|
| Gelsolin | Ca2+ and F-actin |
