通过异核核磁共振光谱法确定Grb2 SH2结构域的化学位移归属和二级结构。
Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy.
作者信息
Wang Y S, Frederick A F, Senior M M, Lyons B A, Black S, Kirschmeier P, Perkins L M, Wilson O
机构信息
Schering-Plough Research Institute, Kenilworth, NJ 07033, USA.
出版信息
J Biomol NMR. 1996 Mar;7(2):89-98. doi: 10.1007/BF00203819.
The growth factor receptor-bound protein-2 (Grb-2) is an adaptor protein that mediates signal transduction pathways. Chemical shift assignments were obtained for the SH2 domain of Grb2 by heteronuclear NMR spectroscopy, employing the uniformly 13C-/15N-enriched protein as well as the protein containing selectively 15N-enriched amino acids. Using the Chemical Shift Index (CSI) method, the chemical shift indices of four nuclei, 1H alpha, 13C alpha, 13C beta and 13CO, were used to derive the secondary structure of the protein. Nuclear Overhauser enhancements (NOEs) were then employed to confirm the secondary structure. The CSI results were compared to the secondary structural elements predicted for the Grb2 SH2 domain from a sequence alignment [Lee et al. (1994) Structure, 2, 423-438]. The core structure of the SH2 domain contains an antiparallel beta-sheet and two alpha-helices. In general, the secondary structural elements determined from the CSI method agree well with those predicted from the sequence alignment.
生长因子受体结合蛋白2（Grb-2）是一种介导信号转导途径的衔接蛋白。通过异核核磁共振光谱法，利用均匀13C-/15N标记的蛋白质以及含有选择性15N标记氨基酸的蛋白质，获得了Grb2的SH2结构域的化学位移归属。使用化学位移指数（CSI）方法，利用四个原子核（1Hα、13Cα、13Cβ和13CO）的化学位移指数来推导蛋白质的二级结构。然后利用核Overhauser效应（NOE）来确认二级结构。将CSI结果与通过序列比对预测的Grb2 SH2结构域的二级结构元件进行比较[Lee等人（1994年），《结构》，2，423 - 438]。SH2结构域的核心结构包含一个反平行β折叠和两个α螺旋。总体而言，通过CSI方法确定的二级结构元件与通过序列比对预测的元件吻合良好。
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