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- Title
Profilin binds proline-rich ligands in two distinct amide backbone orientations.
- Authors
Mahoney, Nicole M.; Rozwarski, Denise A.; Fedorov, Elena; Fedorov, Alexander A.; Almo, Steven C.
- 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.
- Subjects
ACTIN; PROTEINS; PROLINE; X-ray crystallography; LIGANDS (Biochemistry)
- Publication
Nature Structural Biology, 1999, Vol 6, Issue 7, p666
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/10722