A protein phosphatase-1-binding motif identified by the panning of a random peptide display library.
An unusually large number of regulatory or targeting proteins that bind to the catalytic subunit of protein phosphatase-1 have been recently reported. This can be explained by their possession of a common protein motif that interacts with a binding site on protein phosphatase-1. The existence of such a motif was established by the panning of a random peptide library in which peptide sequences are displayed on the Escherichia coli bacterial flagellin protein for bacteria that bound to protein phosphatase-1. There were 79 isolates containing 46 unique sequences with the conserved motif VXF or VXW, where X was most frequently His or Arg. In addition, this sequence was commonly preceded by 2-5 basic residues and followed by 1 acidic residue. This study demonstrates that binding to protein phosphatase-1 can be conferred to a protein by the presentation of a peptide motif on a surface loop. This binding motif is found in a number of protein phosphatase-1-binding proteins.
Zhao
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Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101, USA.
Lee
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EY
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D004926:Escherichia coli; D008969:Molecular Sequence Data; D019151:Peptide Library; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D011485:Protein Binding; D054645:Protein Phosphatase 1; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D019151:Peptide Library; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1