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

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 oligonucleotid...

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Veröffentlicht in:Biomolecular NMR assignments 2009-12, Vol.3 (2), p.261-264
Hauptverfasser: Motácková, Veronika, Kubícková, Monika, Kozísek, Milan, Sasková, Klára Grantz, Svec, Martin, Zídek, Lukás, Sklenár, Vladimír
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Sprache:eng
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Zusammenfassung: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.
ISSN:1874-270X
DOI:10.1007/s12104-009-9189-x