Abstract
The Grb2-like adaptor protein GADS is composed of an N-terminal SH3 domain, an SH2 domain, a proline-rich region and a C-terminal SH3 domain. GADS interacts through its C-terminal SH3 domain with the adaptor protein SLP-76, thus recruiting this protein and other associated molecules to the linker for activation of T-cell (LAT) protein. The DNA encoding the C-terminal SH3 domain of GADS (GADS-cSH3) was assembled synthetically using a recursive PCR technique and the protein was overexpressed in Escherichia coli, refolded and purified. Several crystals of this domain in complex with the SLP-76 peptide were obtained and characterized.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry*
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / isolation & purification
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Amino Acid Motifs
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Animals
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Crystallization
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Crystallography, X-Ray
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Mice
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Phosphoproteins / chemistry*
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Protein Folding*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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src Homology Domains* / genetics
Substances
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Adaptor Proteins, Signal Transducing
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Mona protein, mouse
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Peptide Fragments
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Phosphoproteins
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Recombinant Proteins
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SLP-76 signal Transducing adaptor proteins