BioNMR

BioNMR (http://www.bionmr.com/forum/)
-   Journal club (http://www.bionmr.com/forum/journal-club-9/)
-   -   [NMR paper] Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. (http://www.bionmr.com/forum/journal-club-9/conformation-dynamics-gag-polyprotein-human-immunodeficiency-virus-1-studied-nmr-spectroscopy-22273/)

nmrlearner 06-05-2015 01:57 PM

Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
 
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.

http://www.bionmr.com//www.ncbi.nlm....-pnas_full.gif Related Articles Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.

Proc Natl Acad Sci U S A. 2015 Mar 17;112(11):3374-9

Authors: Deshmukh L, Ghirlando R, Clore GM

Abstract
Assembly and maturation of the human immunodeficiency virus type 1 (HIV-1) are governed by the Gag polyprotein. Here we study the conformation and dynamics of a large HIV-1 Gag fragment comprising the matrix, capsid, spacer peptide 1 and nucleocapsid domains (referred to as ?Gag) by heteronuclear multidimensional NMR spectroscopy. In solution, ?Gag exists in a dynamic equilibrium between monomeric and dimeric states. In the presence of nucleic acids and at low ionic strength ?Gag assembles into immature virus-like particles. The structured domains of ?Gag (matrix, the N- and C-terminal domains of capsid, and the N- and C-terminal zinc knuckles of nucleocapsid) retain their fold and reorient semi-independently of one another; the linkers connecting the structural domains, including spacer peptide 1 that connects capsid to nucleocapsid, are intrinsically disordered. Structural changes in ?Gag upon proteolytic processing by HIV-1 protease, monitored by NMR in real-time, demonstrate that the conformational transition of the N-terminal 13 residues of capsid from an intrinsically disordered coil to a ?-hairpin upon cleavage at the matrix|capsid junction occurs five times faster than cleavage at the capsid|spacer peptide 1 junction. Finally, nucleic acids interact with both nucleocapsid and matrix domains, and proteolytic processing at the spacer peptide 1|nucleocapsid junction by HIV-1 protease is accelerated in the presence of single-stranded DNA.


PMID: 25713345 [PubMed - indexed for MEDLINE]



More...


All times are GMT. The time now is 02:53 PM.

Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013