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Structural Basis for Specific Binding of the Gads SH3 Domain to an RxxK Motif-Containing SLP-76 Peptide

Liu, Qin, Berry, Donna, Nash, Piers, Pawson, Tony, McGlade, C.Jane, Li, Shawn Shun-Cheng·2003·Molecular Cell
DOI 10.1016/s1097-2765(03)00046-7
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Abstract

The SH3 domain, which normally recognizes proline-rich sequences, has the potential to bind motifs with an RxxK consensus. To explore this novel specificity, we have determined the solution structure of the Gads T cell adaptor C-terminal SH3 domain in complex with an RSTK-containing peptide, representing its physiological binding site on the SLP-76 docking protein. The SLP-76 peptide engages four distinct binding pockets on the surface of the Gads SH3 domain and upon binding adopts a unique structure characterized by a right-handed 3(10) helix at the RSTK locus, in contrast to the left-handed polyproline type II helix formed by canonical proline-rich SH3 ligands. The structure, and supporting mutagenesis and peptide binding data, reveal a novel mode of ligand recognition by SH3 domains.

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  • A subfamily of SH3 domains binds atypical peptide ligands centered around a consensus RXXK peptide motif.

    “We and others have previously reported a subfamily of SH3 domains that bind to atypical peptide ligands centered around a consensus RXXK peptide motif (19 -21, 43-46).”

    From Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex (2010) · cites this paper as [43]

  • The second RXXK motif (R2) lacks consensus residues N-terminal to Asp at -1 relative to the conserved arginine but maintains the core DRXXKP region.

    “The second RXXK motif in USP8 (R2) lacks consensus residues N-terminal to Asp located at Ϫ1 relative to the conserved arginine in both species but maintains the core region corresponding to DRXXKP”

    From Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex (2010) · cites this paper as [43]

  • Classical SH3 domains bind to proline-rich ligands that assume a polyproline type II helix, whereas this subfamily of SH3 domains interacts with R-XXK ligands, which take on a characteristic 3_10 helical conformation.

    “Although the classical SH3 domains bind to proline-rich ligands that assume a polyproline type II helix (52), this subfamily of SH3 domains interacts with R-XXK ligands, which take on a characteristic 3 10 helical conformation (43).”

    From Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex (2010) · cites this paper as [43]

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Metadata

Authors
Liu, Q., Berry, D., Nash, P., Pawson, T., McGlade, C. J., & Li, S. S.-C.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2003-02
Volume
11
Issue
2
Pages
471-481
ISSN
1097-2765
DOI
10.1016/s1097-2765(03)00046-7
Cited by
119
References
1
Language
en
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