Structural highlights
Publication Abstract from PubMed
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. How ZAP recognizes its target RNA has been unclear. Here we report the crystal structure of the N-terminal domain of rat ZAP (NZAP225), the major functional domain. The overall structure of NZAP225 resembles a tractor, with four zinc-finger motifs located at the bottom. Structural and functional analyses identified multiple positively charged residues and two putative RNA-binding cavities forming a large putative RNA-binding cleft. ZAP molecules interact to form a dimer that binds to a ZAP-responsive RNA molecule containing two ZAP-binding modules. These results provide insights into how ZAP binds specifically to complex target RNA.
Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA.,Chen S, Xu Y, Zhang K, Wang X, Sun J, Gao G, Liu Y Nat Struct Mol Biol. 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243. PMID:22407013[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen S, Xu Y, Zhang K, Wang X, Sun J, Gao G, Liu Y. Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA. Nat Struct Mol Biol. 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243. PMID:22407013 doi:10.1038/nsmb.2243
