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

MOTÁČKOVÁ, Veronika, Monika KUBÍČKOVÁ, Milan KOŽÍŠEK, Klára GRANTZ ŠAŠKOVÁ, Martin ŠVEC, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. 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. Biomolecular NMR Assignments. Netherlands: Springer Netherlands, 2009, vol. 3, No 2, p. 261-264. ISSN 1874-2718.

Basic information

• Original name: 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
• Name in Czech: 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
• Authors: MOTÁČKOVÁ, Veronika (203 Czech Republic, belonging to the institution), Monika KUBÍČKOVÁ (203 Czech Republic, belonging to the institution), Milan KOŽÍŠEK (203 Czech Republic), Klára GRANTZ ŠAŠKOVÁ (203 Czech Republic), Martin ŠVEC (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution).
• Edition: Biomolecular NMR Assignments, Netherlands, Springer Netherlands, 2009, 1874-2718.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 0.750
• RIV identification code: RIV/00216224:14310/09:00037169
• Organization unit: Faculty of Science
• UT WoS: 000271442700026
• Keywords in English: 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
• Tags: International impact, Reviewed

Abstract

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.

Abstract (in Czech)

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.

Links

• LC06030, research and development project: Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

• MSM0021622413, plan (intention): Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment