Equine infectious anemia virus Tat is a predominantly helical protein.
Eur J Biochem
; 218(3): 973-6, 1993 Dec 15.
Article
em En
| MEDLINE
| ID: mdl-7506657
ABSTRACT
Nuclear magnetic resonance (NMR) spectroscopy revealed features of the secondary structure of the equine infectious anemia virus (EIAV) Tat protein in solution. We could show that this protein, which is required in the replication cycle of lentiviruses, forms a predominantly helical structure in trifluoroethanol/water (40% by vol.) solution. In particular, the basic RNA-binding region and the adjacent core domain, which are highly conserved among lentiviral Tat proteins, show helix-type secondary structure under these conditions. Our observations, in concert with recent biochemical data from other laboratories, suggest that the core sequence region and the basic sequence region form interdependent structural domains, both possibly necessary for correct RNA binding.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Produtos do Gene tat
/
Vírus da Anemia Infecciosa Equina
Idioma:
En
Revista:
Eur J Biochem
Ano de publicação:
1993
Tipo de documento:
Article
País de afiliação:
Alemanha