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Biomol NMR Assign. 2018 Apr;12(1):43-45. doi: 10.1007/s12104-017-9777-0. Epub 2017 Sep 20.

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

Author information

1
Department of Biochemistry, Weill Cornell Medical College, 1300 York Avenue, Box 63, New York, NY, 10065, USA.
2
Instituto Ferreyra (INIMEC-CONICET-Universidad Nacional de Córdoba), Córdoba, Argentina.
3
Department of Biochemistry, Weill Cornell Medical College, 1300 York Avenue, Box 63, New York, NY, 10065, USA. wcb2001@med.cornell.edu.

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.

KEYWORDS:

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

PMID:
28933046
DOI:
10.1007/s12104-017-9777-0

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