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'''PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS''' | '''PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS''' | ||
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[[Category: Mahoney, N M.]] | [[Category: Mahoney, N M.]] | ||
[[Category: Rozwarski, D A.]] | [[Category: Rozwarski, D A.]] | ||
[[Category: | [[Category: Actin-binding protein]] | ||
[[Category: | [[Category: Cytoskeleton]] | ||
[[Category: | [[Category: Poly-l-proline]] | ||
[[Category: | [[Category: Profilin]] | ||
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Revision as of 12:48, 2 May 2008
PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS
OverviewOverview
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 StructureAbout this Structure
1CJF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 12:47:59 2008