Artículo
NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
Fecha de publicación:
04/2018
Editorial:
Springer
Revista:
Biomolecular Nmr Assignments
ISSN:
1874-2718
e-ISSN:
1874-270X
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
BDNF
,
INTRINSICALLY DISORDERED PROTEINS
,
NEUROTROPHIN
,
PRODOMAIN
,
UREA
,
VAL66MET
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(INIMEC - CONICET)
Articulos de INSTITUTO DE INV. MEDICAS MERCEDES Y MARTIN FERREYRA
Articulos de INSTITUTO DE INV. MEDICAS MERCEDES Y MARTIN FERREYRA
Citación
Wang, Jing; Bains, Henrietta; Anastasia Gonzalez, Agustin; Bracken, Clay; NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state; Springer; Biomolecular Nmr Assignments; 12; 1; 4-2018; 43-45
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