The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly prolinerich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.
|Original language||English (US)|
|Number of pages||6|
|Journal||Nature Structural Biology|
|State||Published - 1999|
ASJC Scopus subject areas
- Structural Biology