2ci8
From Proteopedia
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| - | [[Image:2ci8.gif|left|200px]]<br /><applet load="2ci8" size=" | + | [[Image:2ci8.gif|left|200px]]<br /><applet load="2ci8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ci8, resolution 1.80Å" /> | caption="2ci8, resolution 1.80Å" /> | ||
'''SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED'''<br /> | '''SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED'''<br /> | ||
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==Disease== | ==Disease== | ||
| - | Known disease associated with this structure: | + | Known disease associated with this structure: Skin pigmentation, variation in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609802 609802]] |
==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 SO4 and 1PE 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:35:35 2008'' |
Revision as of 08:35, 3 February 2008
|
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 disease associated with this structure: Skin pigmentation, variation in OMIM:[609802]
About this Structure
2CI8 is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . 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
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