NR AXFV
AU Sandhu,N.; Duus,K.; Jorgensen,C.S.; Hansen,P.R.; Bruun,S.W.; Pedersen,L.O.; Hojrup,P.; Houen,G.
TI Peptide binding specificity of the chaperone calreticulin
QU Biochimica et Biophysica Acta 2007 Jun; 1774(6): 701-13
PT journal article; research support, non-u.s. gov't
AB Calreticulin is a molecular chaperone with specificity for polypeptides and N-linked monoglucosylated glycans. In order to determine the specificity of polypeptide binding, the interaction of calreticulin with polypeptides was investigated using synthetic peptides of different length and composition. A large set of available synthetic peptides (n=127) was tested for binding to calreticulin and the results analysed by multivariate data analysis. The parameter that correlated best with binding was hydrophobicity while beta-turn potential disfavoured binding. Only hydrophobic peptides longer than 5 amino acids showed binding and a clear correlation with hydrophobicity was demonstrated for oligomers of different hydrophobic amino acids. Insertion of hydrophilic amino acids in a hydrophobic sequence diminished or abolished binding. In conclusion our results show that calreticulin has a peptide-binding specificity for hydrophobic sequences and delineate the fine specificity of calreticulin for hydrophobic amino acid residues.
MH Amino Acid Sequence; Amino Acids/chemistry/metabolism; Calreticulin/*metabolism; Histocompatibility Antigens Class I/metabolism; Humans; Hydrophobicity; Molecular Chaperones/*metabolism; Molecular Sequence Data; Peptide Fragments/chemistry/*metabolism; Prions/chemistry/metabolism; Protein Binding; Sensitivity and Specificity; Serum Amyloid P-Component/chemistry/metabolism
AD Department of Autoimmunology, Statens Serum Institut, Artillerivej 5, DK-2300 Copenhagen, Denmark.
SP englisch
PO Niederlande