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1awi
From Proteopedia
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| - | [[Image:1awi.gif|left|200px]] | + | [[Image:1awi.gif|left|200px]] |
| - | + | ||
| - | '''HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE''' | + | {{Structure |
| + | |PDB= 1awi |SIZE=350|CAPTION= <scene name='initialview01'>1awi</scene>, resolution 2.2Å | ||
| + | |SITE= <scene name='pdbsite=PPA:Poly-L-PRO+Binding+Site'>PPA</scene> and <scene name='pdbsite=PPB:Poly-L-PRO+Binding+Site'>PPB</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AWI is a [ | + | 1AWI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9360613 9360613] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: profilin]] | [[Category: profilin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:10 2008'' |
Revision as of 08:03, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Sites: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 10:03:10 2008
