2ci8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ci8.gif|left|200px]]<br /><applet load="2ci8" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2ci8.gif|left|200px]]
-
caption="2ci8, resolution 1.80&Aring;" />
+
 
-
'''SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED'''<br />
+
{{Structure
 +
|PDB= 2ci8 |SIZE=350|CAPTION= <scene name='initialview01'>2ci8</scene>, resolution 1.80&Aring;
 +
|SITE= <scene name='pdbsite=AC1:1pe+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
2CI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:1pe+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI8 OCA].
+
2CI8 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=2CI8 OCA].
==Reference==
==Reference==
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16636066 16636066]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/16636066 16636066]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 27: Line 36:
[[Category: binding specificity]]
[[Category: binding specificity]]
[[Category: host-pathogen]]
[[Category: host-pathogen]]
-
[[Category: interactions]]
+
[[Category: interaction]]
[[Category: phosphorylation]]
[[Category: phosphorylation]]
[[Category: sh2-domain]]
[[Category: sh2-domain]]
[[Category: sh3 domain]]
[[Category: sh3 domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:54 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:15:46 2008''

Revision as of 14:15, 20 March 2008


PDB ID 2ci8

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED


Contents

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.

Disease

Known diseases associated with this structure: Skin/hair/eye pigmentation 6, blond/brown hair OMIM:[609840], Skin/hair/eye pigmentation 6, blue/green eyes OMIM:[609840]

About this Structure

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

Reference

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 Thu Mar 20 16:15:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools