Origin of neurotoxins from defensins / 生理学报
Acta Physiologica Sinica
;
(6): 239-247, 2015.
Artículo
en Inglés
| WPRIM
| ID: wpr-255952
ABSTRACT
There are at least three conserved protein folds shared by ion channel-targeted neurotoxins and antimicrobial defensins, including cysteine-stabilized α-helix and β-sheet fold (CSαβ), inhibitor cystine knot fold (ICK) and β-defensin fold (BDF). Based on a combined data of sequences, structures and functions, it has been proposed that these neurotoxins could originate from related ancient antimicrobial defensins by neofunctionalization. This provides an ideal system to study how a novel function emerged from a conserved structural scaffold during evolution. The elucidation of functional novelty of proteins not only has great significance in evolutionary biology but also will be helpful in guiding rational molecular design. This review describes recent progresses in origin of neurotoxins, focusing on the three conserved protein scaffolds.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Química
/
Estructura Secundaria de Proteína
/
Evolución Molecular
/
Defensinas
/
Neurotoxinas
Idioma:
Inglés
Revista:
Acta Physiologica Sinica
Año:
2015
Tipo del documento:
Artículo
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