NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state.
NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state.
复制标题
尿素变性状态下 BDNF 前结构域变体的 NMR 主链共振分配。
DOI：
10.1007/s12104-017-9777-0
复制
发表时间：
2018
影响因子：
0.9
通讯作者：
Bracken,Clay
中科院分区：
文献类型：
--
作者：
Wang,Jing;Bains,Henrietta;Anastasia,Agustin;Bracken,Clay
Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone1H,13C, and15N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2 M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.
