| Literature DB >> 34459989 |
Israel Alshanski1, Deborah E Shalev2,3, Shlomo Yitzchaik4, Mattan Hurevich5.
Abstract
Oxytocin is a neuropeptide that binds copper ions in nature. The structure of oxytocin in interaction with Cu2+ was determined here by NMR, showing which atoms of the peptide are involved in binding. Paramagnetic relaxation enhancement NMR analyses indicated a binding mechanism where the amino terminus was required for binding and subsequently Tyr2, Ile3 and Gln4 bound in that order. The aromatic ring of Tyr2 formed a π-cation interaction with Cu2+. Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses.Entities:
Keywords: Copper complex; Nuclear magnetic resonance; Oxytocin; Paramagnetic resonance enhancement; Peptide
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Year: 2021 PMID: 34459989 DOI: 10.1007/s00775-021-01897-1
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358