3U9G

Crystal structure of the Zinc finger antiviral protein

Summary for 3U9G

• Entry DOI: 10.2210/pdb3u9g/pdb
• Descriptor: Zinc finger CCCH-type antiviral protein 1, ZINC ION (3 entities in total)
• Functional Keywords: zinc finger protein, antiviral protein
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: Q8K3Y6
• Total number of polymer chains: 1
• Total formula weight: 26209.66

Authors

Chen, S.,Xu, Y.,Zhang, K.,Wang, X.,Sun, J.,Gao, G.,Liu, Y. (deposition date: 2011-10-18, release date: 2012-03-14, Last modification date: 2024-03-20)

Primary citation

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., 19:430-435, 2012

PubMed 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.

PubMed: 22407013
DOI: 10.1038/nsmb.2243

Experimental method

X-RAY DIFFRACTION (1.801 Å)