对与B2受体的Fab模拟物结合的重组15N/13C/2H标记的缓激肽进行核磁共振研究。
NMR investigations of recombinant 15N/13C/2H-labeled bradykinin bound to a Fab mimic of the B2 receptor.
作者信息
Ottleben H, Haasemann M, Ramachandran R, Müller-Esterl W, Brown L R
机构信息
Institut für Molekulare Biotechnologie e.V., Jena, Germany.
出版信息
Recept Channels. 1997;5(3-4):237-41.
NMR spectroscopy has been used to obtain structural information on the bioactive conformation of the nonapeptide hormone bradykinin (Arg-Pro-Pro-Gly-Ser-Pro-Phe-Arg, BK) bound to the Fab-fragment of an antibody that mimics the hormone binding site of the natural bradykinin B2-receptor. Using 15N or 15N,13C, 60% 2H isotope labelled bradykinin, complete 1H, 13C and 15N assignments for bradykinin bound to the Fab-fragment have been obtained. Preliminary interpretation of 15N edited NOE spectra indicates that the conformation of bradykinin bound to the model receptor differs substantially from previous computer models of the bioactive conformation of bradykinin.
核磁共振光谱已被用于获取与模拟天然缓激肽B2受体激素结合位点的抗体Fab片段结合的九肽激素缓激肽（精氨酸-脯氨酸-脯氨酸-甘氨酸-丝氨酸-脯氨酸-苯丙氨酸-精氨酸，BK）生物活性构象的结构信息。使用15N或15N、13C、60% 2H同位素标记的缓激肽，已获得与Fab片段结合的缓激肽的完整1H、13C和15N归属。对15N编辑的核Overhauser效应（NOE）光谱的初步解释表明，与模型受体结合的缓激肽构象与先前缓激肽生物活性构象的计算机模型有很大不同。
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