Nature Structural & Molecular Biology, 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243.
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.
State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Abstract
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.
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全文链接：http://www.nature.com/nsmb/journal/v19/n4/full/nsmb.2243.html
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