title: Identification of calmodulin-binding peptide consensus sequences from a phage-displayed random peptide library.
abstract: The calcium-binding protein, calmodulin (CaM), was used to screen a phage library displaying random peptides 26 amino acids (aa) in length. Twenty CaM-binding peptides were identified, 17 of which contained one of three consensus sequence motifs: + W-OlambdaR, WRAAV or WRXXAAAL, where +, -, O, lambda and X are positively charged, negatively charged, hydrophobic, leucine or valine, and any residue, respectively. The Trp residue in these motifs is located within 14 aa of the N-terminus of the displayed peptide. Previous studies [Dedman et al., J. Biol. Chem. 268 (1993) 23025-23030] using a library displaying random peptides 15 aa in length identified CaM-binding peptides which contained a Trp-Pro dipeptide motif. These results suggest that the type of CaM-binding motif identified can vary between different types of combinatorial peptides.
authors.affiliation: Department of Biology, University of North Carolina, Chapel Hill, 27599-3280, USA.
authors.forename: N B
authors.initials: NB
authors.lastname: Adey
authors.forename: B K
authors.initials: BK
authors.lastname: Kay
mesh_terms: D000595:Amino Acid Sequence; D002118:Calcium / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D016384:Consensus Sequence; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D002148:Calmodulin-Binding Proteins; D002118:Calcium