Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00449387" target="_blank" >RIV/61388963:_____/15:00449387 - isvavai.cz</a>

Alternative codes found

RIV/60461373:22330/15:43899471 RIV/60461373:22810/15:43899471

Result on the web

<a href="http://dx.doi.org/10.1007/s12104-014-9580-0" target="_blank" >http://dx.doi.org/10.1007/s12104-014-9580-0</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s12104-014-9580-0" target="_blank" >10.1007/s12104-014-9580-0</a>

Result language

angličtina

Original language name

Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

Original language description

The matrix protein (MA) of the Mason-Pfizer monkey virus (M-PMV) plays a key role in the transport and budding of immature retroviral particles from the host cell. Natural N-terminal myristoylation of MA is essential for the targeting of the particles tothe plasma membrane and participates in the interaction of MA with membranes phospholipids. The mutation Y28F/Y67F in MA reduces budding and thus causes the accumulation of viral particles under the cytoplasmic membrane. To investigate the impact of Y28F/Y67F mutation on the structure of MA, we prepared this protein in amount and quality suitable for NMR spectroscopy. We report backbone, side-chain and myristoyl residue assignments of the Y28F/Y67F mutant of the M-PMV matrix protein, which will be usedto study the interaction with membrane phospholipids and to determine the structure of the mutant matrix protein.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/GAP302%2F12%2F1895" target="_blank" >GAP302/12/1895: Role of retroviral matrix protein in virus particle targeting and interaction with plasma membrane.</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biomolecular NMR Assignments

ISSN

1874-2718

e-ISSN

—

Volume of the periodical

9

Issue of the periodical within the volume

2

Country of publishing house

DE - GERMANY

Number of pages

5

Pages from-to

229-233

UT code for WoS article

000361440100002

EID of the result in the Scopus database

2-s2.0-84941933543