Structural highlights
Function
NEU1_HUMAN Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (PubMed:18174156).[1]
Publication Abstract from PubMed
Oxytocin is a neuropeptide that binds copper ions in nature. The structure of oxytocin in interaction with Cu(2+) 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 pi-cation interaction with Cu(2+). Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses.
Determining the structure and binding mechanism of oxytocin-Cu(2+) complex using paramagnetic relaxation enhancement NMR analysis.,Alshanski I, Shalev DE, Yitzchaik S, Hurevich M J Biol Inorg Chem. 2021 Oct;26(7):809-815. doi: 10.1007/s00775-021-01897-1. Epub , 2021 Aug 30. PMID:34459989[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dutertre S, Croker D, Daly NL, Andersson A, Muttenthaler M, Lumsden NG, Craik DJ, Alewood PF, Guillon G, Lewis RJ. Conopressin-T from Conus tulipa reveals an antagonist switch in vasopressin-like peptides. J Biol Chem. 2008 Mar 14;283(11):7100-8. PMID:18174156 doi:10.1074/jbc.M706477200
- ↑ Alshanski I, Shalev DE, Yitzchaik S, Hurevich M. Determining the structure and binding mechanism of oxytocin-Cu(2+) complex using paramagnetic relaxation enhancement NMR analysis. J Biol Inorg Chem. 2021 Oct;26(7):809-815. PMID:34459989 doi:10.1007/s00775-021-01897-1
