Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.
Proteins
; 81(7): 1266-70, 2013 Jul.
Article
em En
| MEDLINE
| ID: mdl-23508996
ABSTRACT
The NLRP1 inflammasome responds to microbial challenges such as Bacillus anthracis infection and is implicated in autoimmune disease such as vitiligo. Human NLRP1 contains both an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD), with the latter being essential for its association with the downstream effector procaspase-1. Here we report a 2.0 Å crystal structure of the human NLRP1 CARD as a fusion with the maltose-binding protein. The structure reveals the six-helix bundle fold of the NLRP1 CARD, typical of the death domain superfamily. The charge surface of the NLRP1 CARD structure and a procaspase-1 CARD model suggests potential mechanisms for their association through electrostatic attraction.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ligação Proteica
/
Caspase 1
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Proteínas Adaptadoras de Transdução de Sinal
/
Proteínas Reguladoras de Apoptose
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article