PDF(Pubmed)
Abstract：
The splicing isoform b of human fibroblast growth factor 8 (FGF8b) is an important regulator of brain embryonic development. Here, we report the almost complete NMR chemical shift assignment of the backbone and aliphatic side chains of FGF8b. Obtained chemical shifts are in good agreement with the previously reported X-ray data, excluding the N-terminal gN helix, which apparently forms only in complex with the receptor. The reported data provide an NMR starting point for the investigation of FGF8b interaction with its receptors and with potential drugs or inhibitors.
摘要：
人成纤维细胞生长因子8（FGF8b）的剪接亚型b是脑胚胎发育的重要调节因子。这里,我们报道了FGF8b的主链和脂肪族侧链的几乎完整的NMR化学位移分配。获得的化学位移与先前报道的X射线数据非常吻合，不包括N端gN螺旋，显然只与受体复合形成。报道的数据为研究FGF8b与其受体和潜在药物或抑制剂的相互作用提供了NMR起点。
