1cjf: Difference between revisions

Revision as of 20:50, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cjf.png

Template:STRUCTURE 1cjf

PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONSPROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS

Template:ABSTRACT PUBMED 10404225

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 Mon Jun 30 20:50:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1cjf.gif|left|200px]]
+{{Seed}}
+[[Image:1cjf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1cjf|  PDB=1cjf  |  SCENE=  }}
-'''PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS'''
+===PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_10404225}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10404225 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10404225}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Poly-l-proline]]
 [[Category: Profilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:47:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:50:00 2008''