1cf0

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[[Image:1cf0.gif|left|200px]]
[[Image:1cf0.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf0 OCA], [http://www.ebi.ac.uk/pdbsum/1cf0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cf0 RCSB]</span>
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'''HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE'''
'''HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE'''
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[[Category: Mahoney, N M.]]
[[Category: Mahoney, N M.]]
[[Category: Rozwarski, D A.]]
[[Category: Rozwarski, D A.]]
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[[Category: actin cytoskeleton]]
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[[Category: Actin cytoskeleton]]
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[[Category: complex (actin-binding protein/peptide)]]
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[[Category: Poly-l-proline]]
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[[Category: poly-l-proline]]
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[[Category: Profilin]]
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[[Category: profilin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:29 2008''
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Revision as of 09:39, 2 May 2008

Template:STRUCTURE 1cf0

HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE


Overview

The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.

About this Structure

1CF0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Profilin binds proline-rich ligands in two distinct amide backbone orientations., Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC, Nat Struct Biol. 1999 Jul;6(7):666-71. PMID:10404225 Page seeded by OCA on Fri May 2 12:39:38 2008

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