Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization

. 2009 Oct 10 ; 393 (1) : 168-76. [epub] 20090822

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid19699504

Grantová podpora
CA 27834 NCI NIH HHS - United States

Odkazy

PubMed 19699504
DOI 10.1016/j.virol.2009.07.014
PII: S0042-6822(09)00449-8
Knihovny.cz E-zdroje

The Mason-Pfizer monkey virus is a prototype Betaretrovirus with the defining characteristic that it assembles spherical immature particles from Gag-related polyprotein precursors within the cytoplasm of the infected cell. It was shown previously that the N-terminal part of the Gag p12 domain (wt-Np12) is required for efficient assembly. However, the precise role for p12 in mediating Gag-Gag interaction is still poorly understood. In this study we employed detailed circular dichroism spectroscopy, electron microscopy and ultracentrifugation analyses of recombinant wt-Np12 prepared by in vitro transcription and translation. The wt-Np12 domain fragment forms fibrillar structures in a concentration-dependent manner. Assembly into fibers is linked to a conformational transition from unfolded or another non-periodical state to alpha-helix during multimerization.

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