2D0N

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

Summary for 2D0N

• Entry DOI: 10.2210/pdb2d0n/pdb
• Related: 1H3H 1OEB 1UJ0 1UTI
• Descriptor: GRB2-related adaptor protein 2, SLP-76 binding peptide (3 entities in total)
• Functional Keywords: sh3 domain-complex, mona/gads sh3c domain, signaling protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 15443.22

Authors

Dimasi, N. (deposition date: 2005-08-04, release date: 2005-08-23, Last modification date: 2023-10-25)

Primary citation

Dimasi, N.
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., 39:109-123, 2007

PubMed 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.

PubMed: 17010654
DOI: 10.1016/j.biocel.2006.07.003

Experimental method

X-RAY DIFFRACTION (1.57 Å)