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

* Residue conservation analysis

PDB id:

2d0n

Name:

Signaling protein

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

Structure:

Grb2-related adaptor protein 2. Chain: a, c. Fragment: c-terminal sh3 domain. Synonym: gads protein, growth factor receptor binding protein, grblg, grb-2-like protein, grb2l, hematopoietic cell-associated adaptor protein grpl, grb-2-related monocytic adapter protein, monocytic adapter, mona, adapter protein grid. Engineered: yes. Slp-76 binding peptide.

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: the slp-76 peptide was synthesized synthetically with the f-moc chemistry

Biol. unit:

Tetramer (from PQS)

Resolution:

1.57Å R-factor: 0.221 R-free: 0.284

Authors:

N.Dimasi

Key ref:

N.Dimasi (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, 109-123. PubMed id: 17010654 DOI: 10.1016/j.biocel.2006.07.003

Date:

04-Aug-05 Release date: 23-Aug-05

Protein chain

O89100  (GRAP2_MOUSE) -  GRB2-related adaptor protein 2 from Mus musculus

Seq: 322 a.a.

Struc: 59 a.a.*

Protein chain

O89100  (GRAP2_MOUSE) -  GRB2-related adaptor protein 2 from Mus musculus

Seq: 322 a.a.

Struc: 56 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, C: E.C.?

DOI no: 10.1016/j.biocel.2006.07.003

Int J Biochem Cell Biol 39:109-123 (2007)

PubMed id: 17010654

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.

N.Dimasi.

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.