Profilin binds proline-rich ligands in two distinct amide backbone orientations.
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Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC
Profilin binds proline-rich ligands in two distinct amide backbone orientations.
Nat Struct Biol. 1999 Jul;6(7):666-71.
- PubMed ID
- 10404225 [ View in PubMed]
- Abstract
The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich 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.