1awi: Difference between revisions

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[[Image:1awi.gif|left|200px]]
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{{STRUCTURE_1awi|  PDB=1awi  |  SCENE=  }}  
{{STRUCTURE_1awi|  PDB=1awi  |  SCENE=  }}  


'''HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE'''
===HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Poly-l-proline]]
[[Category: Poly-l-proline]]
[[Category: Profilin]]
[[Category: Profilin]]
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Revision as of 17:45, 30 June 2008

File:1awi.png

Template:STRUCTURE 1awi

HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDEHUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE

Template:ABSTRACT PUBMED 9360613

About this StructureAbout this Structure

1AWI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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