| Primary Identifier | IPR014828 | Type | Domain |
| Short Name | NSP7_CoV |
| description | Non-structural protein NSP7 has been implicated in viral RNA replication and is predominantly α-helical in structure. Its central core is an N-terminal helical bundle (HB), with helices HB1, HB2 and HB3, forming a triple-stranded antiparallel coiled coil with a right-handed superhelical pitch. It is part of the RNA-dependent RNA polymerase (RdRp) heterotetramer which consists of one NSP7, two NSP8 molecules and the catalytic NSP12, defined as the minimal core component for mediating coronavirus RNA synthesis [, , , , , ]. NSP7 and NSP8 forms a complex that adopts a hollow cylinder-like structure []. The dimensions of the central channel and positive electrostatic properties of the cylinder imply that it confers processivity on RNA-dependent RNA polymerase []. NSP7 and NSP8 play a role in the stabilisation of NSP12 regions involved in RNA binding, and are essential for a highly active NSP12 polymerase complex [, , , ]. |
