1H3H
Structural Basis for Specific Recognition of an RxxK-containing SLP-76 peptide by the Gads C-terminal SH3 domain
Summary for 1H3H
| Entry DOI | 10.2210/pdb1h3h/pdb |
| Descriptor | GRB2-RELATED ADAPTOR PROTEIN 2, LYMPHOCYTE CYTOSOLIC PROTEIN 2 (2 entities in total) |
| Functional Keywords | protein-binding, complex (sh3-peptide), t-cell signaling, sh3 domain, sh2 domain, protein binding |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Nucleus (By similarity): O89100 |
| Total number of polymer chains | 2 |
| Total formula weight | 8093.09 |
| Authors | Liu, Q.,Berry, D.,Nash, P.,Pawson, T.,McGlade, C.J.,Li, S.S. (deposition date: 2002-09-03, release date: 2003-03-06, Last modification date: 2024-05-15) |
| Primary citation | Liu, Q.,Berry, D.,Nash, P.,Pawson, T.,Mcglade, C.J.,Li, S.S. Structural Basis for Specific Binding of the Gads SH3 Domain to an Rxxk Motif-Containing Slp-76 Peptide: A Novel Mode of Peptide Recognition Mol.Cell, 11:471-, 2003 Cited by PubMed 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. PubMed: 12620234DOI: 10.1016/S1097-2765(03)00046-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
