Abstract
Profilin, a ubiquitous low molecular weight (13,000-15,000 M(r)) actin binding protein, regulates the formation of F-actin structures in vivo, and is localized to specific cellular regions through interaction with proline- rich sequences. Here we report the 2.2 Å X-ray structure of the complex between human platelet profilin (HPP) and a decamer of L-proline (L-Pro10). The L-Pro10 peptide adopts a left-handed type II poly-L-proline helix (PPiI) and binds to a highly conserved patch of aromatic amino acids on the surface of profilin. The peptide and actin binding sites reside on orthogonal surfaces, and L-Pro10 binding does not result in a conformational rearrangement of HPP. This structure suggests a mechanism for the localization of profilin and its actin-related activities to sites of actin filament assembly in vivo.
Original language | English (US) |
---|---|
Pages (from-to) | 953-960 |
Number of pages | 8 |
Journal | Nature Structural Biology |
Volume | 4 |
Issue number | 11 |
DOIs | |
State | Published - 1997 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics