1egx: Difference between revisions

Revision as of 00:40, 1 July 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:1egx.png

Template:STRUCTURE 1egx

SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

Template:ABSTRACT PUBMED 10990454

About this StructureAbout this Structure

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

ReferenceReference

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity., Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T, EMBO J. 2000 Sep 15;19(18):4903-14. PMID:10990454

Page seeded by OCA on Tue Jul 1 00:40:56 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1egx.jpg|left|200px]]
+{{Seed}}
+[[Image:1egx.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1egx|  PDB=1egx  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)'''
+===SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)===
-==Overview==
+<!--
-The Ena-VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N-terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide interactions are strongly dependent on the recognition of residues flanking the core FPPPP motifs. Determination of the VASP EVH1 domain solution structure, together with peptide library screening, measurement of individual K(d)s by fluorescence titration, and NMR chemical shift mapping, revealed a second affinity-determining epitope present in all four ActA EVH1-binding motifs. The epitope was shown to interact with a complementary hydrophobic site on the EVH1 surface and to increase strongly the affinity of ActA for EVH1 domains. We propose that this epitope, which is absent in the sequences of the native EVH1-interaction partners zyxin and vinculin, may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell.
+The line below this paragraph, {{ABSTRACT_PUBMED_10990454}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10990454 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10990454}}
 ==About this Structure==
-EGX 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=1EGX OCA].
+EGX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA].
 ==Reference==
@@ Line 38: / Line 42: @@
 [[Category: Poly-proline-binding domain]]
 [[Category: Vasp-ena]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:05:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:40:56 2008''