Novel interaction partners of the CD2BP2-GYF domain.
The GYF domain of CD2BP2 serves as an adapter that recognizes proline-rich sequences in intracellular proteins. Although the T cell adhesion molecule CD2 and the core splicing protein SmB/B' were previously shown to interact with CD2BP2-GYF, we are now using a general approach to identify putative GYF domain target sites ... within the human proteome. The phage display-derived recognition motif for CD2BP2-GYF is PPG(W/F/Y/M/L). SPOT analysis confirmed that the GYF domain interacts with peptides from human proteins containing the consensus site. Epitope mapping by NMR spectroscopy performed for several peptides revealed a conserved binding surface. A direct interaction of the CD2BP2-GYF domain with the novel protein interaction partners PI31 and NPWBP was verified by yeast two-hybrid analysis.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Arginine, Carrier Proteins, Chromatography, High Pressure Liquid, Conserved Sequence, Databases as Topic, Glutathione Transferase, Humans, Hydrophobic and Hydrophilic Interactions, Lysine, Mass Spectrometry, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Library, Peptides, Proline, Protein Structure, Secondary, Protein Structure, Tertiary, Proteome, Recombinant Fusion Proteins, Trifluoroacetic Acid, Two-Hybrid System Techniques, Water
Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Arginine, Carrier Proteins, Chromatography, High Pressure Liquid, Conserved Sequence, Databases as Topic, Glutathione Transferase, Humans, Hydrophobic and Hydrophilic Interactions, Lysine, Mass Spectrometry, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Library, Peptides, Proline, Protein Structure, Secondary, Protein Structure, Tertiary, Proteome, Recombinant Fusion Proteins, Trifluoroacetic Acid, Two-Hybrid System Techniques, Water
J. Biol. Chem.
Date: Sep. 30, 2005
PubMed ID: 16000308
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