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 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.
Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic.
Veronika
V
Motácková
Monika
M
Kubícková
Milan
M
Kozísek
Klára Grantz
KG
Sasková
Martin
M
Svec
Lukás
L
Zídek
Vladimír
V
Sklenár
D000818:Animals; D007426:Genes, Intracisternal A-Particle; D051379:Mice; D019906:Nuclear Magnetic Resonance, Biomolecular; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D012190:Retroviridae / Q000201:enzymology*
D010447:Peptide Hydrolases