Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis,JBIC Journal of Biological Inorganic Chemistry

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Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis
JBIC Journal of Biological Inorganic Chemistry ( IF 2.7 ) Pub Date : 2021-08-30 , DOI: 10.1007/s00775-021-01897-1
Israel Alshanski ₁ , Deborah E Shalev _{2,

3} , Shlomo Yitzchaik ₁ , Mattan Hurevich ₁

Affiliation

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⁺.

Graphic abstract

Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses

中文翻译：

使用顺磁弛豫增强核磁共振分析确定催产素-Cu2+ 复合物的结构和结合机制

催产素是一种在自然界中与铜离子结合的神经肽。在此通过NMR确定催产素与Cu ²⁺相互作用的结构，显示肽的哪些原子参与结合。顺磁弛豫增强核磁共振分析表明了一种结合机制，其中氨基末端是结合所必需的，随后 Tyr2、Ile3 和 Gln4 以该顺序结合。^{Tyr2的芳香环与Cu 2+}形成π-阳离子相互作用。

图形摘要

顺磁弛豫增强核磁共振分析揭示催产素铜络合物结构

更新日期：2021-08-30

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