Please use this identifier to cite or link to this item:
|Title:||The disordered N-terminal region of dengue virus capsid protein contains a lipid-droplet-binding motif|
|Authors:||Martins, Ivo C.|
Faustino, André F.
Carvalho, Filomena A.
Carneiro, Fabiana A.
Bozza, Patricia T.
Castanho, Miguel A. R. B.
Almeida, Fábio C. L.
Santos, Nuno C.
Da Poian, Andrea T.
|Keywords:||Atomic force microscopy (AFM)|
Dengue virus (DENV)
Intrinsically disordered protein
|Citation:||Biochem. J. (2012) 444, 405–415|
|Abstract:||Dengue is the major arthropod-borne human viral disease, for which no vaccine or specific treatment is available. We used NMR, zeta potential measurements and atomic force microscopy to study the structural features of the interaction between dengue virus C (capsid) protein and LDs (lipid droplets), organelles crucial for infectious particle formation. C protein-binding sites to LD were mapped, revealing a new function for a conserved segment in the N-terminal disordered region and indicating that conformational selection is involved in recognition. The results suggest that the positively charged N-terminal region of C protein prompts the interaction with negatively charged LDs, after which a conformational rearrangement enables the access of the central hydrophobic patch to the LD surface. Taken together, the results allowed the design of a peptide with inhibitory activity of C protein–LD binding, paving the way for new drug development approaches against dengue.|
|Description:||©The Authors Journal compilation ©2012 Biochemical Society - 'The final version of record is available at http://www.biochemj.org/bj/|
|Appears in Collections:||IMM - Artigos em Revistas Internacionais|
Files in This Item:
|Biochem_J_PtnC.pdf||1,15 MB||Adobe PDF||View/Open Request a copy|
|Supplement.pdf||208,95 kB||Adobe PDF||View/Open Request a copy|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.