PDBsum entry 2d0n

Signaling protein

PDB id: 2d0n

Contents

Protein chains

59 a.a.

56 a.a.

Ligands

PRO-SER-ILE-ASP-ARG-SER-THR-LYS-PRO ×2

Waters ×199

References listed in PDB file

Key reference

• Title: 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.
• Author: N.Dimasi.
• Ref.: Int J Biochem Cell Biol, 2007, 39, 109-123. [DOI no: 10.1016/j.biocel.2006.07.003]
• PubMed id: 17010654

Abstract

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.