2d0n
From Proteopedia
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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
Overview
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.
About this Structure
2D0N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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., Dimasi N, Int J Biochem Cell Biol. 2007;39(1):109-23. Epub 2006 Aug 12. PMID:17010654
Page seeded by OCA on Wed Nov 21 09:22:57 2007
