| First Author | Dimasi N | Year | 2007 |
| Journal | Int J Biochem Cell Biol | Volume | 39 |
| Issue | 1 | Pages | 109-23 |
| PubMed ID | 17010654 | Mgi Jnum | J:201258 |
| Mgi Id | MGI:5512843 | Doi | 10.1016/j.biocel.2006.07.003 |
| Citation | Dimasi N (2007) Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction. Int J Biochem Cell Biol 39(1):109-23 |
| abstractText | The Grb2-like adaptor protein GADS is essential for tyrosine kinase-dependent signaling in T lymphocytes. Following T cell receptor ligation, GADS interacts through its C-terminal SH3 domain with the adaptors SLP-76 and LAT, to form a multiprotein signaling complex that is crucial for T cell activation. To understand the structural basis for the selective recognition of GADS by SLP-76, herein is reported the crystal structure at 1.54 Angstrom of the C-terminal SH3 domain of GADS bound to the SLP-76 motif 233-PSIDRSTKP-241, which represents the minimal binding site. In addition to the unique structural features adopted by the bound SLP-76 peptide, the complex structure reveals a unique SH3-SH3 interaction. This homophilic interaction, which is observed in presence of the SLP-76 peptide and is present in solution, extends our understanding of the molecular mechanisms that could be employed by modular proteins to increase their signaling transduction specificity. |
