2ci8: Difference between revisions

Revision as of 03:57, 29 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:2ci8.png

Template:STRUCTURE 2ci8

SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXEDSH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED

Template:ABSTRACT PUBMED 16636066

About this StructureAbout this Structure

2CI8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src homology 2 domains., Frese S, Schubert WD, Findeis AC, Marquardt T, Roske YS, Stradal TE, Heinz DW, J Biol Chem. 2006 Jun 30;281(26):18236-45. Epub 2006 Apr 24. PMID:16636066

Page seeded by OCA on Tue Jul 29 03:57:36 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ci8.gif|left|200px]]
+{{Seed}}
+[[Image:2ci8.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ci8|  PDB=2ci8  |  SCENE=  }}
-'''SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED'''
+===SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED===
-==Overview==
+<!--
-Nck proteins are essential Src homology (SH) 2 and SH3 domain-bearing adapters that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. Two mammalian pathogens, enteropathogenic Escherichia coli and vaccinia virus, exploit Nck as part of their infection strategy. Conflicting data indicate potential differences in the recognition specificities of the SH2 domains of the isoproteins Nck1 (Nckalpha) and Nck2 (Nckbeta and Grb4). We have characterized the binding specificities of both SH2 domains and find them to be essentially indistinguishable. Crystal structures of both domains in complex with phosphopeptides derived from the enteropathogenic E. coli protein Tir concur in identifying highly conserved, specific recognition of the phosphopeptide. Differential peptide recognition can therefore not account for the preference of either Nck in particular signaling pathways. Binding studies using sequentially mutated, high affinity phosphopeptides establish the sequence variability tolerated in peptide recognition. Based on this binding motif, we identify potential new binding partners of Nck1 and Nck2 and confirm this experimentally for the Arf-GAP GIT1.
+The line below this paragraph, {{ABSTRACT_PUBMED_16636066}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16636066 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16636066}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Sh2-domain]]
 [[Category: Sh3 domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Apr 29 12:17:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:57:36 2008''