1CJF

Profilin binds proline-rich ligands in two distinct amide backbone orientations.

(1999) Nat Struct Biol 6: 666-671

• PubMed: 10404225 Search on PubMed
• DOI: https://doi.org/10.1038/10722
• Primary Citation of Related Structures:  
  1CF0, 1CJF


• 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.

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Organizational Affiliation: 

Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.