Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
Copyright policy )Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
The WW domain is a new protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. It is present in a number of signalling and regulatory proteins, often in several copies. Here we investigate the solution structure of the WW domain of human YAP65 (for Yes kinase-associated protein) in complex with proline-rich peptides containing the core motif PPxY. The structure of the domain with the bound peptide GTPPPPYTVG is a slightly curved, three-stranded, antiparallel beta-sheet. Two prolines pack against the first tryptophan, forming a hydrophobic buckle on the convex side of the sheet. The concave side has three exposed hydrophobic residues (tyrosine, tryptophan and leucine) which form the binding site for the ligand. A non-conserved isoleucine in the amino-terminal flanking region covers a hydrophobic patch and stabilizes the WW domain of human YAP65 in vitro. The structure of the WW domain differs from that of the SH3 domain and reveals a new design for a protein module that uses stacked aromatic surface residues to arrange a binding site for proline-rich peptides.
Models, Molecular, Proline, Protein Conformation, Molecular Sequence Data, Cell Cycle Proteins, Protein Structure, Secondary, Mice, Consensus Sequence, Animals, Humans, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, Binding Sites, Sequence Homology, Amino Acid, Phosphoproteins, Proline-Rich Protein Domains, Carrier Proteins, Peptides, Protein Binding, Transcription Factors
Models, Molecular, Proline, Protein Conformation, Molecular Sequence Data, Cell Cycle Proteins, Protein Structure, Secondary, Mice, Consensus Sequence, Animals, Humans, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, Binding Sites, Sequence Homology, Amino Acid, Phosphoproteins, Proline-Rich Protein Domains, Carrier Proteins, Peptides, Protein Binding, Transcription Factors
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