Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.
J Biol Chem
; 289(18): 12535-49, 2014 May 02.
Article
em En
| MEDLINE
| ID: mdl-24668816
ABSTRACT
Coronavirus envelope (CoV E) proteins are â¼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted ß-coil-ß motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted ß-coil-ß motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Transdução de Sinais
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Proteínas do Envelope Viral
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Coronavírus Relacionado à Síndrome Respiratória Aguda Grave
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Complexo de Golgi
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article