Alshanski Israel, Shalev Deborah E, Yitzchaik Shlomo, Hurevich Mattan
Institute of Chemistry and Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, 91904, Jerusalem, Israel.
Department of Pharmaceutical Engineering, Azrieli College of Engineering Jerusalem, 91035, Jerusalem, Israel.
J Biol Inorg Chem. 2021 Oct;26(7):809-815. doi: 10.1007/s00775-021-01897-1. Epub 2021 Aug 30.
Oxytocin is a neuropeptide that binds copper ions in nature. The structure of oxytocin in interaction with Cu 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 Cu. Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses.
催产素是一种在自然界中能结合铜离子的神经肽。本文通过核磁共振（NMR）确定了催产素与铜相互作用时的结构，显示了肽链中的哪些原子参与了结合。顺磁弛豫增强核磁共振分析表明了一种结合机制，即结合需要氨基末端，随后依次是酪氨酸2（Tyr2）、异亮氨酸3（Ile3）和谷氨酰胺4（Gln4）结合。酪氨酸2的芳香环与铜形成了π-阳离子相互作用。顺磁弛豫增强核磁共振分析揭示了催产素铜复合物的结构。
