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

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Authors	MOTÁČKOVÁ Veronika KUBÍČKOVÁ Monika KOŽÍŠEK Milan GRANTZ ŠAŠKOVÁ Klára ŠVEC Martin ŽÍDEK Lukáš SKLENÁŘ Vladimír
Year of publication	2009
Type	Article in Periodical
Magazine / Source	Biomolecular NMR Assignments
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	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
Attached files	2009_Bio_NMR_Assign_Motackova_etal.pdf
Description	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.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre