NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state Academic Article uri icon

Overview

MeSH Major

  • Chloride Channels
  • Chlorides
  • Ion Pumps
  • Proteolipids

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 (1)H, (13)C, and (15)N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2┬áM 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.

publication date

  • September 20, 2017

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1007/s12104-017-9777-0

PubMed ID

  • 28933046

Additional Document Info

start page

  • 1

end page

  • 3