| Description | The exact function of the Hepatitis C non-structural 5A (NS5A) protein is not known, but it is an active component of the replicase, regulates replication and modulates a range of cellular processes including innate immunity and dysregulated cell growth. NS5A is organised into three domains, labelled I, II and III. Domain I contains a zinc-binding motif and an amphipathic N-terminal helix which promotes membrane association. Mutations disrupting either the membrane anchor or zinc binding are lethal for RNA replication [ , ].This entry represents the 1b domain of NS5A. It consists of two distinct anti-parallel β-sheets surrounded by extensive random coil structures [ ]. This domain contains a disulphide bond near its C-terminal not required for the RNA replicase functions of NS5A. The presence of the cited sulphide bond suggests that it is likely responsible of the structural arrangement of domains II and III, thus playing a regulatory role in NS5A function by serving as a conformation switch to modulate functions of NS5A in and out of the replicase []. | Name | Hepatitis C virus non-structural 5a, 1B domain |
| Short Name | HCV_NS5a_1B_dom | Type | Domain |
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