Nucleocapsid protein of HIV-1 and its Zn2+complex formation analysis with electrospray mass spectrometry
- 26 October 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 311 (3), 259-262
- https://doi.org/10.1016/0014-5793(92)81115-3
Abstract
The Zn2+ binding properties of the synthetic nucleocapsid protein (Ncp7) of HIV-1, containing two zinc-binding domains, have been studied using electrospray mass spectrometry (ES-MS). ES-MS measurements revealed strong binding of Zn2+ by Ncp7. Its shorter fragments, Ncp7-(1–35)- and (29–55)-peptides, each containing only one zinc-binding domain, bind one equivalent of Zn2+ ions tightly. ES-MS studies allows these fragments to be distinguished in terms of their binding affinity: they showed stronger binding of Zn2+ by Ncp7-(1–35)-peptide. Surprisingly, in addition to the expected two zinc-binding domains, a third metal binding site was detected in Ncp7. However, this site appears to bind different metal ions without selectivity and most probably reflects salt formation at the C-terminal acidic residuesKeywords
This publication has 6 references indexed in Scilit:
- First large scale chemical synthesis of the 72 amino acid HIV-1 nucleocapsid protein NCp7 in an active formBiochemical and Biophysical Research Communications, 1991
- Electrospray: Its potential and limitations as an ionization method for biomoleculesJournal of Mass Spectrometry, 1990
- The nucleocapsid protein isolated from HIV-1 particles binds zinc and forms retroviral-type zinc fingersBiochemistry, 1990
- High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approachBiochemistry, 1990
- Ion spray interface for combined liquid chromatography/atmospheric pressure ionization mass spectrometryAnalytical Chemistry, 1987
- Potential Metal-Binding Domains in Nucleic Acid Binding ProteinsScience, 1986