A possible calcium binding site in animal lectins: a 1H-NMR study of the interaction between lanthanides and a synthetic peptide from a highly conserved domain of Pleurodeles lectin.
1H-NMR techniques have been used to study the metal binding properties of a synthetic peptide of 15 amino acids corresponding to a highly conserved domain of Pleurodeles lectin. The addition of lanthanum chloride or praseodymium chloride in a peptide solution induces some conformational changes as displayed by several concerted variations of peptide resonances. The Ln3+ concentration dependence of the chemical shifts was used to calculate the Ln3+ binding constants. The dissociation constants of 95 microM and 280 microM were found for La3+ and Pr3+, respectively.
Bondon
A
A
Laboratoire de Chimie Organométallique et Biologique, URA CNRS No. 415, Université de Rennes I, France.
Tiffoche
C
C
Simonneaux
G
G
Le Pennec
J P
JP
Jego
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D003001:Cloning, Molecular; D006801:Humans; D006859:Hydrogen; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008674:Metals, Rare Earth / Q000378:metabolism*; D008969:Molecular Sequence Data; D010999:Pleurodeles; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D037102:Lectins; D008674:Metals, Rare Earth; D006859:Hydrogen; D002118:Calcium