Application | Comment | Organism |
---|---|---|
additional information | domain movements between NS3 protease and NS3 helicase result in the regulation of its activities. NS3 protease increases the stability of subdomain 1 of the RNA helicase. Upon release of the carboxy-terminus from NS3 protease, the residues involved in this interaction are folded back into the last alpha helix. Slow collective motions of NS3. The two lowest-frequency normal modes are enough to describe reorientations of NS3 protease relative to NS3 helicase. Movements induce an increment in the exposure of the active site of NS3 protease that can be important during the proteolytic processing of the viral polyprotein. The third low-frequency normal mode is correlated to subdomain reorientations of NS3 helicase | Dengue virus |
additional information | domain movements between NS3 protease and NS3 helicase result in the regulation of its activities. NS3 protease increases the stability of subdomain 1 of the RNA helicase. Upon release of the carboxy-terminus from NS3 protease, the residues involved in this interaction are folded back into the last alpha helix. Slow collective motions of NS3. The two lowest-frequency normal modes are enough to describe reorientations of NS3 protease relative to NS3 helicase. Movements induce an increment in the exposure of the active site of NS3 protease that can be important during the proteolytic processing of the viral polyprotein. The third low-frequency normal mode is correlated to subdomain reorientations of NS3 helicase | Hepacivirus C |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Dengue virus | - |
- |
- |
Hepacivirus C | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
non-structural 3 protein | - |
Dengue virus |
non-structural 3 protein | - |
Hepacivirus C |
NS3 | - |
Dengue virus |
NS3 | - |
Hepacivirus C |
NS3 protease | - |
Dengue virus |
NS3 protease | - |
Hepacivirus C |