Zinc and copper bind to unique sites of histatin 5
Open Access
- 20 February 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 491 (1-2) , 76-80
- https://doi.org/10.1016/s0014-5793(01)02157-3
Abstract
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...Keywords
This publication has 26 references indexed in Scilit:
- Evaluation of the metal binding properties of the histidine-rich antimicrobial peptides histatin 3 and 5 by electrospray ionization mass spectrometryRapid Communications in Mass Spectrometry, 2000
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- Zn2+Ions Selectively Induce Antimicrobial Salivary Peptide Histatin-5 To Fuse Negatively Charged Vesicles. Identification and Characterization of a Zinc-Binding Motif Present in the Functional DomainBiochemistry, 1999
- NMR studies of the antimicrobial salivary peptides histatin 3 and histatin 5 in aqueous and nonaqueous solutionsBiochemistry and Cell Biology, 1998
- Slow conformational dynamics at the metal coordination site of a zinc fingerJournal of the American Chemical Society, 1991
- Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalisBiochemical and Biophysical Research Communications, 1991
- A unique signature identifies a family of zinc‐dependent metallopeptidasesFEBS Letters, 1989
- Histidine residues of Lactobacillus casei dihydrofolate reductase: paramagnetic relaxation and deuterium-exchange studies and partial assignmentsBiochemistry, 1980
- Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119Biochemistry, 1975