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 Cited by 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: 9360613DOI: 10.1038/nsb1197-953 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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