NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state

作者：Wang Jing; Bains Henrietta; Anastasia Agustin; Bracken Clay^*

来源：Biomolecular NMR Assignments, 2018, 12(1): 43-45.

DOI：10.1007/s12104-017-9777-0

• BDNF
• Val66Met
• Prodomain
• Neurotrophin
• Urea
• Intrinsically disordered proteins

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 backbone H-1, C-13, and N-15 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.

• 出版日期2018-4