| http://purl.uniprot.org/citations/23219468 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23219468 | http://www.w3.org/2000/01/rdf-schema#comment | "Itk (interleukin-2 inducible T cell kinase) is a non-receptor protein tyrosine kinase expressed primarily in T cells. Itk catalyzes phosphorylation on tyrosine residues within a number of its natural substrates, including the well-characterized Y783 of PLCγ1. However, the molecular mechanisms Itk exploits to recognize its substrates are not completely understood. We have previously identified a specific docking interaction between the kinase domain of Itk and the C-terminal Src homology 2 (SH2C) domain of PLCγ1 that promotes substrate specificity for this enzyme/substrate pair. In the current study, we identify and map the interaction surface on the Itk kinase domain as an acidic patch centered on the G helix. Mutation of the residues on and adjacent to the G helix within the Itk kinase domain impairs the catalytic efficacy of PLCγ1 substrate phosphorylation by specifically altering the protein-protein interaction interface and not the inherent catalytic activity of Itk. NMR titration experiments using a Btk (Bruton's tyrosine kinase) kinase domain as a surrogate for the Itk kinase domain provide further support for an Itk/PLCγ1 SH2C interaction surrounding the G helix of the kinase domain. The work presented here provides structural insight into how the Itk kinase uses the G helix to single out Y783 of PLCγ1 for specific phosphorylation. Comparing these results to other well-characterized kinase/substrate systems suggests that the G helix is a general structural feature used by kinases for substrate recognition during signaling."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2012.10.023"xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/author | "Xie Q."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/author | "Fulton D.B."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/author | "Joseph R.E."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/author | "Andreotti A.H."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/pages | "683-696"xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/title | "Substrate recognition of PLCgamma1 via a specific docking surface on Itk."xsd:string |
| http://purl.uniprot.org/citations/23219468 | http://purl.uniprot.org/core/volume | "425"xsd:string |
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