Induction of a Secondary Structure in the N-Terminal Pentadecapeptide of Human Protamine HP2 through Ni(II) Coordination. An NMR Study

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• 作者：Wojciech Bal ; Jacek Wó ; jcik ; Maciej Maciejczyk ; Pawe//pubs.acs.org/images/entities/lstrok.gif" border="0"> Grochowski ; and Kazimierz S. Kasprzak
• 刊名：Chemical Research in Toxicology
• 出版年：2000
• 出版时间：September 2000
• 年：2000
• 卷：13
• 期：9
• 页码：823 - 830
• 全文大小：423K
• 年卷期：v.13,no.9(September 2000)
• ISSN：1520-5010

文摘

A solution structure of the Ni(II) complex with the N-terminal pentadecapeptide of humanprotamine HP2 (HP2_1-15) was elucidated with the use of a range of one- and two-dimensional¹H NMR techniques and molecular modeling. A striking double-loop conformation was found,exhibiting the interactions of the aromatic ring of the Tyr⁸ residue with the Ni(II) coordinationsite at Arg¹, Thr², and His³ residues and the side chain of the Arg¹⁵ residue. In such aconformation, a tendency was found for all five positively charged arginine side chains to locateon 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 ofa possible physiological function of the N-terminus of HP2 as a metal-binding site.