A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein

Journal of Biomolecular Structure & Dynamics
Min Lu, P S Kim

Abstract

HIV-1 infection is initiated by the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell. The HIV-1 transmembrane envelope glycoprotein gp41 plays a major role in this membrane fusion process. Previous studies have shown that a stable, alpha-helical, trimeric structural domain of gp41 consists of N-terminal 51-residue (N-51) and C-terminal 43-residue (C-43) extraviral segments. This alpha-helical, trimeric complex has been proposed to form the core of the membrane fusion-active conformation of the HIV-1 envelope. We show here that a stable subdomain can be formed by shorter 36-residue (N-36) and 34-residue (C-34) peptides corresponding to the central regions of N-51 and C-43, respectively. In isolation, N-36 is predominantly aggregated, while C-34 is unfolded. Upon mixing, however, these peptides form a stable, alpha-helical, discrete trimer of heterodimers (the melting temperature of a 10 microM solution is 64 degrees C at pH 7). Thus, this subdomain displays the salient features of the stable core structure of the isolated gp41 protein. Our results also provide strong support for the notion that short peptides can form unique, cooperatively folded subdomains, in which element...Continue Reading

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Citations

Sep 11, 2012·Amino Acids·Yu BaiKeliang Liu
May 26, 2005·Biochemical and Biophysical Research Communications·Ling NiPo Tien
Jul 11, 2006·Journal of Combinatorial Chemistry·Yang XuKim D Janda
Jan 11, 2003·Biotechnology & Genetic Engineering Reviews·Mark A BaumeisterDavid B Weiner
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Jun 9, 2014·The Journal of Antimicrobial Chemotherapy·Huihui ChongYuxian He

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