Zinc and copper bind to unique sites of histatin 5

FEBS Letters

Oppenheim, Frank G.²  McKnight, C.James¹  Grogan, James²  Troxler, Robert F.² 

[1] Boston University Medical Center, Department of Physiology and Biophysics, Boston, MA 02118, USA;Boston University Medical Center, Department of Periodontology and Oral Biology, Boston, MA 02118, USA

关键词: Histatin;    Zinc;    Copper;    Antimicrobial peptide;    Nuclear magnetic resonance;    Protein binding;    Saliva;   

DOI  :  10.1016/S0014-5793(01)02157-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Metal binding has been suggested to be relevant in the antifungal and antibacterial mechanism of histatin 5, a human salivary protein. Proton nuclear magnetic resonance (NMR) spectra were obtained to investigate the specificity of metal binding to the seven histidyl, one aspartyl and one glutamyl amino acid side-chains of histatin 5 in aqueous solutions. Three C^ϵ1–H histidyl and the C^γ–H glutamyl resonances of histatin 5 were selectively altered in spectra of solutions containing three equivalents of zinc. Copper binding to histatin 5 resulted in a reduced intensity of C^β–H aspartyl resonances, while no evidence for calcium binding was found. These results indicate that zinc binding to histatin 5 involves His-15 present within the –H–E–X–X–H– zinc binding motif, and copper binding occurs within the N-terminal D–S–H–, ATCUN motif.

【 授权许可】

Unknown