We report here the crystal structure of MNV NS6 pro, which has been determined to a resolution of 1.6 Å. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6 pro within the peptide-binding cleft of a neighbouring molecule.

Jul 14, 2021 · We report here the crystal structure of MNV NS6 (pro), which has been determined to a resolution of 1.6 Å. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6 (pro) within the peptide-binding cleft of a neighbouring molecule.

We report the crystallization and crystal structure determination of inactive mutants of murine norovirus NS6 protease with C-terminal extensions of one, two and four residues from the N-terminus of the adjacent NS7 protein (NS6 1′, NS6 2′, NS6 4′).

Feb 26, 2015 · We report the crystallization and crystal structure determination of inactive mutants of murine norovirus NS6 protease with C-terminal extensions of one, two and four residues from the N-terminus of the adjacent NS7 protein (NS6 1', NS6 2', NS6 4').

We report the crystallization and crystal structure determination of inactive mutants of murine norovirus NS6 protease with C-terminal extensions of one, two and four residues from the N-terminus of the adjacent NS7 protein (NS6 1′, NS6 2′, NS6 4′).

We report here the crystal structure of MNV NS6pro, which has been determined to a resolution of 1.6 A ̊. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6pro within the peptide-binding cleft of a neighbouring molecule.

May 5, 2013 · NS6 protease is involved in proteolytic processing of the non-structural (NS) polyprotein precursor encoded in the norovirus genome RNA, and is crucial for viral replication.

Aug 16, 2022 · We discovered that selective polyprotein processing of the murine norovirus polyprotein shields MNV from restriction by the host antiviral protein Trim7. Trim7 can bind the viral protein NS6 but not the viral precursor protein NS6-7.

Mar 15, 2019 · NS6 (also known as Pro, 3C-like) and NS7 (3DPol, RdRP) encode the 3C-like protease and RNA-dependent RNA polymerase, respectively. The N-terminal 3 proteins are less well characterized but are known to localize to cytoplasmic membranes.

Jun 7, 2012 · In this report we extend the structural work on noroviral proteases by describing the X-ray structure of full-length MNV NS6 pro. Fortuitously the structure has been solved in a crystal form in which the C-terminus of one protease extends into the active site of another.