Open AccessExpression, refolding and crystallizations of the Grb2‐like (GADS) C‐terminal SH3 domain complexed with a SLP‐76 motif peptide
Author(s) -
Faravelli Alessandro,
Dimasi Nazzareno
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105041023
Subject(s) - grb2 , sh3 domain , signal transducing adaptor protein , linker , peptide , chemistry , hamp domain , ww domain , proteogenomics , protein domain , biochemistry , signal transduction , proto oncogene tyrosine protein kinase src , gene , gene expression , computer science , transcriptome , operating system
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.