1awi
From Proteopedia
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HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE
Overview
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.
About this Structure
1AWI is a Single protein structure of sequence from Homo sapiens. Structure known Active Sites: PPA and PPB. Full crystallographic information is available from OCA.
Reference
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation., Mahoney NM, Janmey PA, Almo SC, Nat Struct Biol. 1997 Nov;4(11):953-60. PMID:9360613
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