1AWI

HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE

Summary for 1AWI

• Entry DOI: 10.2210/pdb1awi/pdb
• Descriptor: PROFILIN, L-PRO10 (3 entities in total)
• Functional Keywords: profilin, poly-l-proline, actin cytoskeleton, complex (actin-binding protein-peptide), complex (actin-binding protein-peptide) complex, complex (actin-binding protein/peptide)
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 30727.05

Authors

Mahoney, N.M.,Almo, S.C. (deposition date: 1997-10-02, release date: 1998-10-28, Last modification date: 2024-02-07)

Primary citation

Mahoney, N.M.,Janmey, P.A.,Almo, S.C.
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation.
Nat.Struct.Biol., 4:953-960, 1997

PubMed 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 A 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.

PubMed: 9360613
DOI: 10.1038/nsb1197-953

Experimental method

X-RAY DIFFRACTION (2.2 Å)