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.
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Acknowledgements
The authors thank B. L. Hempstead for helpful discussions and experimental support. This work was supported by the NIH NS090322, RR023694 (to C.B.). Parts of this work were carried out at the New York Structural Biology Center (NYSBC), a NYSTAR Facility.
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Wang, J., Bains, H., Anastasia, A. et al. NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state. Biomol NMR Assign 12, 43–45 (2018). https://doi.org/10.1007/s12104-017-9777-0
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DOI: https://doi.org/10.1007/s12104-017-9777-0