Molecular and structural characterization of the domain 2 of Hepatitis C virus non-structural protein 5A
Kang, Cong Bao
Yoon, Ho Sup
Date of Issue2006
School of Biological Sciences
Hepatitis C virus (HCV) non-structural protein 5A protein (NS5A), which consists of three functional domains, is involved in regulating viral replication, interferon resistance, and apoptosis. Recently, the three-dimensional structure of the domain 1 was determined. However, currently the molecular basis for the domains 2 and 3 of HCV NS5A is yet to be defined. Toward this end, we expressed, purified the domain 2 of the NS5A (NS5A-D2), and then performed biochemical and structural studies. The purified domain 2 was active and was able to bind NS5B and PKR, biological partners of NS5A. The results from gel filtration, CD analysis, 1D 1H NMR and 2D 1H-15N heteronuclear single quantum correlation (HSQC) spectroscopy indicate that the domain 2 of NS5A appears to be flexible and disordered.
Molecules and cells
© 2006 KSMCB. This is the author created version of a work that has been peer reviewed and accepted for publication by Molecules and Cells, KSMCB. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://www.molcells.org/home/journal/].