Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis

Citation:

Alshanski, I. ; Shalev, D. E. ; Yitzchaik, S. ; Hurevich, M. . Determining The Structure And Binding Mechanism Of Oxytocin-Cu2+ Complex Using Paramagnetic Relaxation Enhancement Nmr Analysis. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY 2021, 26, 809-815.

Date Published:

OCT

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 pi-cation interaction with Cu2+Y. 

 


 

 

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Last updated on 09/04/2023