1cjf: Difference between revisions

New page: left|200px<br /> <applet load="1cjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjf, resolution 2.3Å" /> '''PROFILIN BINDS PROLI...
 
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[[Image:1cjf.gif|left|200px]]<br />
[[Image:1cjf.gif|left|200px]]<br /><applet load="1cjf" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1cjf" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1cjf, resolution 2.3&Aring;" />
caption="1cjf, resolution 2.3&Aring;" />
'''PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS'''<br />
'''PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS'''<br />


==Overview==
==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.
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==
==About this Structure==
1CJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HOM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJF OCA].  
1CJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HOM:'>HOM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJF OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Almo, S.C.]]
[[Category: Almo, S C.]]
[[Category: Fedorov, A.A.]]
[[Category: Fedorov, A A.]]
[[Category: Fedorov, E.]]
[[Category: Fedorov, E.]]
[[Category: Mahoney, N.M.]]
[[Category: Mahoney, N M.]]
[[Category: Rozwarski, D.A.]]
[[Category: Rozwarski, D A.]]
[[Category: HOM]]
[[Category: HOM]]
[[Category: actin-binding protein]]
[[Category: actin-binding protein]]
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[[Category: profilin]]
[[Category: profilin]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:43 2008''

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