Induction of a secondary structure in the N-terminal pentadecapeptide of human protamine HP2 through Ni(II) coordination. An NMR study.
A solution structure of the Ni(II) complex with the N-terminal pentadecapeptide of human protamine HP2 (HP2(1)(-)(15)) was elucidated with the use of a range of one- and two-dimensional (1)H NMR techniques and molecular modeling. A striking double-loop conformation was found, exhibiting the interactions of the aromatic ring of the Tyr(8) residue with the Ni(II) coordination site at Arg(1), Thr(2), and His(3) residues and the side chain of the Arg(15) residue. In such a conformation, a tendency was found for all five positively charged arginine side chains to locate on one side of the molecule, making possible efficient contacts with the DNA double helix. These structural features, induced indirectly by Ni(II) coordination, are discussed in terms of a possible physiological function of the N-terminus of HP2 as a metal-binding site.
Bal
W
W
Faculty of Chemistry, University of Wroclaw, Wroclaw, Poland. wbal@wchuwr.chem.uni.wroc.pl
Wójcik
J
J
Maciejczyk
M
M
Grochowski
P
P
Kasprzak
K S
KS
D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009532:Nickel / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011479:Protamines / Q000737:chemistry*; D017433:Protein Structure, Secondary
D011479:Protamines; D009532:Nickel