Liu Dengfeng, Seuthe Alexandra B, Ehrler Oli T, Zhang Xiaohua, Wyttenbach Thomas, Hsu Jeffrey F, Bowers Michael T
Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, California 93106, USA.
J Am Chem Soc. 2005 Feb 23;127(7):2024-5. doi: 10.1021/ja046042v.
Biologists have observed that the presence of divalent metal is essential for the binding of the hormone oxytocin (OT) to its cellular receptor. However, this interaction is not understood on the molecular level. Because conformation is a key factor controlling ligand binding in biomolecule systems, we have used ion mobility experiments and molecular modeling to probe the conformation of the oxytocin-zinc complex. Results show that Zn2+ occupies an octahedral site in the interior of the OT peptide that frees the N-terminus and creates a structured hydrophobic binding site on the peptide exterior; both factors are conducive to binding oxytocin to its receptor.
生物学家观察到,二价金属的存在对于激素催产素(OT)与其细胞受体的结合至关重要。然而,这种相互作用在分子水平上尚不明确。由于构象是控制生物分子系统中配体结合的关键因素,我们利用离子迁移实验和分子建模来探究催产素 - 锌复合物的构象。结果表明,Zn2 +占据OT肽内部的八面体位点,该位点使N端游离,并在肽外部形成一个结构化的疏水结合位点;这两个因素都有利于催产素与其受体的结合。