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

ABSTRACT: 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 1H, 13C, and 15N 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.

SUBMITTER: Wang J

PROVIDER: S-EPMC6865803 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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

Wang Jing J Bains Henrietta H Anastasia Agustin A Bracken Clay C

Biomolecular NMR assignments 20170920 1

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 neurop ...[more]

PMID: 28933046

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