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1awi

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1awi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awi OCA], [http://www.ebi.ac.uk/pdbsum/1awi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1awi RCSB]</span>
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[[Category: profilin]]
[[Category: profilin]]
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Revision as of 15:48, 30 March 2008


PDB ID 1awi

Drag the structure with the mouse to rotate
, resolution 2.2Å
Sites: and
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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