| First Author | Faravelli A | Year | 2006 |
| Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun | Volume | 62 |
| Issue | Pt 1 | Pages | 52-5 |
| PubMed ID | 16511262 | Mgi Jnum | J:200295 |
| Mgi Id | MGI:5508254 | Doi | 10.1107/S1744309105041023 |
| Citation | Faravelli A, et al. (2006) Expression, refolding and crystallizations of the Grb2-like (GADS) C-terminal SH3 domain complexed with a SLP-76 motif peptide. Acta Crystallogr Sect F Struct Biol Cryst Commun 62(Pt 1):52-5 |
| abstractText | The Grb2-like adaptor protein GADS is composed of an N-terminal SH3 domain, an SH2 domain, a proline-rich region and a C-terminal SH3 domain. GADS interacts through its C-terminal SH3 domain with the adaptor protein SLP-76, thus recruiting this protein and other associated molecules to the linker for activation of T-cell (LAT) protein. The DNA encoding the C-terminal SH3 domain of GADS (GADS-cSH3) was assembled synthetically using a recursive PCR technique and the protein was overexpressed in Escherichia coli, refolded and purified. Several crystals of this domain in complex with the SLP-76 peptide were obtained and characterized. |
