Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA

Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses such as HIV-1 by targeting viral mRNA for degradation. Structural analysis now reveals a large RNA-binding surface comprising many positively charged residues and two cavities, thereby providing insight into how ZAP recognizes its target RNA.