Informace o publikaci
Backbone 1H, 13C, and 15N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR
| Autoři | |
|---|---|
| Rok publikování | 2009 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Biomolecular NMR Assignments |
| Fakulta / Pracoviště MU | |
| Citace | |
| Obor | Biochemie |
| Klíčová slova | Retroviral protease; Murine intracisternal A-type particles; inMIA-14 PR; C-terminal domain; Homodimer; Assignment A-type particles \and inMIA-14 PR \and C-terminal domain; Homodimer; Assignment |
| Přiložené soubory | |
| Popis | 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 oligo-nucleotides (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 13Cbeta side chain resonances of the 34\,kDa homo-dimeric inMIA-14 PR is presented in this study. |
| Související projekty: |