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

Veronika Motácková; Monika Kubícková; Milan Kozísek; Klára Grantz Sasková; Martin Svec; Lukás Zídek; Vladimír Sklenár

doi:10.1007/s12104-009-9189-x

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

Biomol NMR Assign. 2009 Dec;3(2):261-4. doi: 10.1007/s12104-009-9189-x.

Authors

Veronika Motácková¹, Monika Kubícková, Milan Kozísek, Klára Grantz Sasková, Martin Svec, Lukás Zídek, Vladimír Sklenár

Affiliation

¹ Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic.

PMID: 19856131
DOI: 10.1007/s12104-009-9189-x

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 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Genes, Intracisternal A-Particle*
Mice
Nuclear Magnetic Resonance, Biomolecular
Peptide Hydrolases / chemistry*
Peptide Hydrolases / genetics*
Peptide Hydrolases / metabolism
Retroviridae / enzymology*

Substances

Peptide Hydrolases