NMR study of non-structural proteins--part II: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Venezuelan equine encephalitis virus (VEEV).
Biomol NMR Assign
; 9(2): 247-51, 2015 Oct.
Article
en En
| MEDLINE
| ID: mdl-25291978
ABSTRACT
Macro domains consist of 130-190 amino acid residues and appear to be highly conserved in all kingdoms of life. Intense research on this field has shown that macro domains bind ADP-ribose and other similar molecules, but their exact function still remains intangible. Macro domains are highly conserved in the Alphavirus genus and the Venezuelan equine encephalitis virus (VEEV) is a member of this genus that causes fatal encephalitis to equines and humans. In this study we report the high yield recombinant expression and preliminary solution NMR study of the macro domain of VEEV. An almost complete sequence-specific assignment of its (1)H, (15)N and (13)C resonances was obtained and its secondary structure predicted by TALOS+. The protein shows a unique mixed α/ß-fold.
Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Proteínas no Estructurales Virales
/
Resonancia Magnética Nuclear Biomolecular
/
Virus de la Encefalitis Equina Venezolana
/
Espectroscopía de Resonancia Magnética con Carbono-13
/
Espectroscopía de Protones por Resonancia Magnética
País/Región como asunto:
America do sul
/
Venezuela
Idioma:
En
Revista:
Biomol NMR Assign
Asunto de la revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Año:
2015
Tipo del documento:
Article
País de afiliación:
Grecia