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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
V Motackova, M Kubickova, M Kozisek, KG Saskova, M Svec, L Zidek, V Sklenar
Jazyk angličtina Země Nizozemsko
Typ dokumentu práce podpořená grantem
- MeSH
- geny pro IAP elementy MeSH
- myši MeSH
- nukleární magnetická rezonance biomolekulární MeSH
- proteasy genetika chemie metabolismus MeSH
- Retroviridae MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- práce podpořená grantem MeSH
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.
Citace poskytuje Crossref.org
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- $a Motáčková, Veronika. $7 _AN067435 $u Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic
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- $a 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.
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