Backbone (1)H, (13)C, and (15)N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR.
Biomol NMR Assign
; 3(2): 261-4, 2009 Dec.
Article
em En
| MEDLINE
| ID: mdl-19856131
ABSTRACT
Proteases play a crucial role in the retroviral infection but so far the mechanism of their regulation remains unclear. Protease MIA-14 from murine intracisternal A-type particles, containing a C-terminal domain rich in glycines (G-patch), is responsible for binding of single-stranded oligonucleotides (both RNA and DNA) without inhibiting the proteolytic activity. For investigations of untill now poorly characterized protease-oligonucleotide interactions, assignments of the observed NMR frequencies are mandatory. An almost complete assignments of the main chain and (13)C(beta) side chain resonances of the 34 kDa homo-dimeric inMIA-14 PR is presented in this study.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeo Hidrolases
/
Retroviridae
/
Genes de Partícula A Intracisternal
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article