D-苯丙氨酸2残基对内源性神经肽阿查丁-I分子构象的影响。阿查丁-I（H-甘氨酸-D-苯丙氨酸-丙氨酸-天冬氨酸-OH）与阿查丁-II（H-甘氨酸-苯丙氨酸-丙氨酸-天冬氨酸-OH）的X射线晶体结构比较。
Effect of the D-Phe2 residue on molecular conformation of an endogenous neuropeptide achatin-I. Comparison of X-ray crystal structures of achatin-I (H-Gly-D-Phe-Ala-Asp-OH) and achatin-II (H-Gly-Phe-Ala-Asp-OH).
作者信息
Ishida T, In Y, Inoue M, Yasuda-Kamatani Y, Minakata H, Iwashita T, Nomoto K
机构信息
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
出版信息
FEBS Lett. 1992 Aug 3;307(3):253-6. doi: 10.1016/0014-5793(92)80689-e.
The molecular conformation of achatin-II neutral form (H-Gly-Phe-Ala-Asp-OH), an endogenous peptide from the Achatina fulica ganglia, was elucidated by X-ray crystal analysis. The molecule takes an extended beta-pleated structure stabilized by 5 intermolecular hydrogen bonds with the antiparallely arranged molecules. This is in contrast with the turn conformation of a neuroactive achatin-I (H-Gly-D-Phe-Ala-Asp-OH) [(1992) FEBS Lett. 276,95-97]. The conformational comparison of both of the molecules makes clear the structural role which D-Phe residue of achatin-I plays in forming a definite active form.
通过X射线晶体分析阐明了来自褐云玛瑙螺神经节的内源性肽——玛瑙螺毒素II中性形式（H-Gly-Phe-Ala-Asp-OH）的分子构象。该分子呈伸展的β-折叠结构，通过与反平行排列分子形成的5个分子间氢键得以稳定。这与具有神经活性的玛瑙螺毒素I（H-Gly-D-Phe-Ala-Asp-OH）的转角构象形成对比[（1992年）《欧洲生物化学学会联合会快报》276, 95 - 97]。对这两种分子的构象比较明确了玛瑙螺毒素I的D-苯丙氨酸残基在形成特定活性形式中所起的结构作用。
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