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NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain.
Biomolecular NMR Assignments ( IF 0.9 ) Pub Date : 2019-04-26 , DOI: 10.1007/s12104-019-09894-x
Karoline Sanches 1 , Ícaro P Caruso 1, 2 , Fábio C L Almeida 2 , Fernando A Melo 1
Affiliation  

Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein composed of three domains, an N-terminal SH3 (nSH3), SH2 and a C-terminal SH3 (cSH3) domains. This multi-domain protein has been reported to be a key factor in many signaling pathways related to controlling cell survival, differentiation, and growth. The Grb2-SH2 domain has been a focus for the study of the interaction with peptides and small molecules to act as inhibitors in uncontrolled cell growth, and consequently inhibit tumor proliferation. Here we describe the almost complete assignment of the free SH2 domain at pH 7. This work prepares the ground for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. TalosN secondary structure prediction showed great similarity with the available structures in the PDB.

中文翻译:

游离1H,15N和13C-Grb2-SH2域的NMR分配。

生长因子受体结合蛋白2(Grb2)是由三个域组成的衔接蛋白,分别是N末端SH3(nSH3),SH2和C末端SH3(cSH3)域。据报道,这种多结构域蛋白是许多与控制细胞存活,分化和生长有关的信号通路中的关键因素。Grb2-SH2结构域一直是研究与肽和小分子相互作用以在不受控制的细胞生长中起抑制剂作用,从而抑制肿瘤增殖的研究重点。在这里,我们描述了pH为7的游离SH2域的几乎完全分配。这项工作为进一步的结构研究,骨架动力学,相互作用图谱以及药物筛选和开发奠定了基础。TalosN二级结构预测显示与PDB中的可用结构非常相似。
更新日期:2019-04-26
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