3u9g | pdb_00003u9g

Crystal structure of the Zinc finger antiviral protein

spinqualitylabelsall models 3u9g, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u9g is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Gene: Zc3hav1, Zap (Rattus norvegicus) Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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