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

N. M. Mahoney, D. A. Rozwarski, E. Fedorov, A. A. Fedorov, S. C. Almo

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)666-671
Number of pages6
JournalNature structural biology
Volume6
Issue number7
DOIs
StatePublished - Jan 1 1999

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ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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